|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5561 |
| Enzyme 1 Name |
Kynureninase |
| Enzyme 1 Synonyms |
- L-kynurenine hydrolase
|
| Enzyme 1 Gene Name |
KYNU |
| Enzyme 1 Protein Sequence |
>Kynureninase
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ALVGWFGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMKALRKK
SVLLTGYLEYLIKHNYGKDKAATKKPVVNIITPSHVEERGCQLTITFSVPNKDVFQELEK
RGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDSAETKN
|
| Enzyme 1 Number of Residues |
465 |
| Enzyme 1 Molecular Weight |
52351.1 |
| Enzyme 1 Theoretical pI |
7.04 |
| Enzyme 1 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on acid carbon-carbon bonds
- hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
- kynureninase activity
- pyridoxal phosphate binding
|
| Process |
- NAD biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- indolalkylamine metabolic process
- metabolic process
- nicotinamide nucleotide biosynthetic process
- pyridine nucleotide biosynthetic process
- tryptophan catabolic process
- tryptophan metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 1 General Function |
Involved in metabolic process |
| Enzyme 1 Specific Function |
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- L-kynurenine + H2O = anthranilate + L-alanine [RN:R00987]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q16719  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
KYNU_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1398 bp
ATGGAGCCTTCATCTCTTGAGCTGCCGGCTGACACAGTGCAGCGCATTGCGGCTGAACTC
AAATGCCACCCAACGGATGAGAGGGTGGCTCTCCACCTAGATGAGGAAGATAAGCTGAGG
CACTTCAGGGAGTGCTTTTATATTCCCAAAATACAGGATCTGCCTCCAGTTGATTTATCA
TTAGTGAATAAAGATGAAAATGCCATCTATTTCTTGGGAAATTCTCTTGGCCTTCAACCA
AAAATGGTTAAAACATATCTTGAAGAAGAACTAGATAAGTGGGCCAAAATAGCAGCCTAT
GGTCATGAAGTGGGGAAGCGTCCTTGGATTACAGGAGATGAGAGTATTGTAGGCCTTATG
AAGGACATTGTAGGAGCCAATGAGAAAGAAATAGCCCTAATGAATGCTTTGACTGTAAAT
TTACATCTTCTAATGTTATCATTTTTTAAGCCTACGCCAAAACGATATAAAATTCTTCTA
GAAGCCAAAGCCTTCCCTTCTGATCATTATGCTATTGAGTCACAACTACAACTTCACGGA
CTTAACATTGAAGAAAGTATGCGGATGATAAAGCCAAGAGAGGGGGAAGAAACCTTAAGA
ATAGAGGATATCCTTGAAGTAATTGAGAAGGAAGGAGACTCAATTGCAGTGATCCTGTTC
AGTGGGGTGCATTTTTACACTGGACAGCACTTTAATATTCCTGCCATCACAAAAGCTGGA
CAAGCGAAGGGTTGTTATGTTGGCTTTGATCTAGCACATGCAGTTGGAAATGTTGAACTC
TACTTACATGACTGGGGAGTTGATTTTGCCTGCTGGTGTTCCTACAAGTATTTAAATGCA
GGAGCAGGAGGAATTGCTGGTGCCTTCATTCATGAAAAGCATGCCCATACGATTAAACCT
GCATTAGTGGGATGGTTTGGCCATGAACTCAGCACCAGATTTAAGATGGATAACAAACTG
CAGTTAATCCCTGGGGTCTGTGGATTCCGAATTTCAAATCCTCCCATTTTGTTGGTCTGT
TCCTTGCATGCTAGTTTAGAGATCTTTAAGCAAGCGACAATGAAGGCATTGCGGAAAAAA
TCTGTTTTGCTAACTGGCTATCTGGAATACCTGATCAAGCATAACTATGGCAAAGATAAA
GCAGCAACCAAGAAACCAGTTGTGAACATAATTACTCCGTCTCATGTAGAGGAGCGGGGG
TGCCAGCTAACAATAACATTTTCTGTTCCAAACAAAGATGTTTTCCAAGAACTAGAAAAA
AGAGGAGTGGTTTGTGACAAGCGGAATCCAAATGGCATTCGAGTGGCTCCAGTTCCTCTC
TATAATTCTTTCCATGATGTTTATAAATTTACCAATCTGCTCACTTCTATACTTGACTCT
GCAGAAACAAAAAATTAG
|
| Enzyme 1 GenBank Gene ID |
U57721  |
| Enzyme 1 GeneCard ID |
KYNU  |
| Enzyme 1 GenAtlas ID |
KYNU  |
| Enzyme 1 HGNC ID |
HGNC:6469  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2q22.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Alberati-Giani D, Buchli R, Malherbe P, Broger C, Lang G, Kohler C, Lahm HW, Cesura AM: Isolation and expression of a cDNA clone encoding human kynureninase. Eur J Biochem. 1996 Jul 15;239(2):460-8. [PubMed
]
- Toma S, Nakamura M, Tone S, Okuno E, Kido R, Breton J, Avanzi N, Cozzi L, Speciale C, Mostardini M, Gatti S, Benatti L: Cloning and recombinant expression of rat and human kynureninase. FEBS Lett. 1997 May 12;408(1):5-10. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Walsh HA, Botting NP: Purification and biochemical characterization of some of the properties of recombinant human kynureninase. Eur J Biochem. 2002 Apr;269(8):2069-74. [PubMed
]
- Lima S, Khristoforov R, Momany C, Phillips RS: Crystal structure of Homo sapiens kynureninase. Biochemistry. 2007 Mar 13;46(10):2735-44. Epub 2007 Feb 15. [PubMed
]
- Christensen M, Duno M, Lund AM, Skovby F, Christensen E: Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase. J Inherit Metab Dis. 2007 Apr;30(2):248-55. Epub 2007 Mar 1. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5633 |
| Enzyme 2 Name |
Alanine--glyoxylate aminotransferase 2, mitochondrial |
| Enzyme 2 Synonyms |
- AGT 2
- (R)-3-amino-2-methylpropionate--pyruvate transaminase
- Beta-ALAAT II
- Beta-alanine-pyruvate aminotransferase
- D-AIBAT
|
| Enzyme 2 Gene Name |
AGXT2 |
| Enzyme 2 Protein Sequence |
>Alanine--glyoxylate aminotransferase 2, mitochondrial
MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS
LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH
PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM
ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH
CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK
GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA
VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK
LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT
FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
|
| Enzyme 2 Number of Residues |
514 |
| Enzyme 2 Molecular Weight |
57155.9 |
| Enzyme 2 Theoretical pI |
7.91 |
| Enzyme 2 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in transaminase activity |
| Enzyme 2 Specific Function |
L-alanine + glyoxylate = pyruvate + glycine |
| Enzyme 2 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 2 Reactions |
- L-alanine + glyoxylate = pyruvate + glycine [RN:R00369]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
12406973  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9BYV1  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
AGT2_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1545 bp
ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG
ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC
AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC
CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA
TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA
GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC
CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC
TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT
CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG
GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC
AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG
ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC
TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA
GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA
ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG
GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT
GAAGTGCAGACAGGATTTGGAAGGTTGGGCTCTCACTTCTGGGGCTTCCAAACCCACGAT
GTCCTGCCTGACATTGTCACCATGGCTAAAGGGATTGGGAATGGCTTTCCCATGGCAGCA
GTCATAACCACTCCAGAGATTGCCAAATCTTTGGCGAAATGCCTGCAGCACTTCAACACC
TTTGGAGGGAACCCCATGGCCTGTGCCATTGGATCTGCTGTGCTTGAGGTGATTAAAGAA
GAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTACTAAAGTTTGCTAAG
CTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGTCTCATGATAGGCATA
GAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAAGAAGTAAATCAGATC
CATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGCATTTTTTCTCAGACA
TTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGATTTTGCAGTAGAAGTA
TTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA
|
| Enzyme 2 GenBank Gene ID |
AJ292204  |
| Enzyme 2 GeneCard ID |
AGXT2  |
| Enzyme 2 GenAtlas ID |
AGXT2  |
| Enzyme 2 HGNC ID |
HGNC:14412  |
| Enzyme 2 Chromosome Location |
5 |
| Enzyme 2 Locus |
5p13 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5897 |
| Enzyme 3 Name |
Alanyl-tRNA synthetase, cytoplasmic |
| Enzyme 3 Synonyms |
- Alanine--tRNA ligase
- AlaRS
- Renal carcinoma antigen NY-REN-42
|
| Enzyme 3 Gene Name |
AARS |
| Enzyme 3 Protein Sequence |
>Alanyl-tRNA synthetase, cytoplasmic
MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPS
HPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALE
LLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGD
TGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNREADGILKPLPKKSIDT
GMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLAD
HARTITVALADGGRPDNTGRGYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDA
FPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGF
PVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEV
TDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGG
QIYDEGYLVKVDDSSEDKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRP
IMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMI
EAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSV
EFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAK
VKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKR
VLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKIT
CLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQ
LRLGDVKN
|
| Enzyme 3 Number of Residues |
968 |
| Enzyme 3 Molecular Weight |
106809.5 |
| Enzyme 3 Theoretical pI |
5.18 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- alanine-tRNA ligase activity
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- alanyl-tRNA aminoacylation
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 3 General Function |
Involved in nucleotide binding |
| Enzyme 3 Specific Function |
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction:alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla [RN:R03038]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
109148542  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P49588  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SYAC_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2907 bp
ATGGACTCTACTCTAACAGCAAGTGAAATCCGGCAGCGATTTATAGATTTCTTCAAGAGG
AACGAGCATACGTATGTTCACTCGTCTGCCACCATCCCATTGGATGACCCCACTTTGCTC
TTTGCCAATGCAGGCATGAACCAGTTTAAACCCATTTTCCTGAACACAATTGACCCATCT
CACCCCATGGCAAAGCTGAGCAGAGCTGCCAATACCCAGAAGTGCATCCGGGCTGGGGGC
AAACATAATGACCTGGACGATGTGGGCAAGGATGTCTATCATCACACCTTCTTCGAGATG
CTGGGCTCTTGGTCTTTTGGAGATTACTTTAAGGAATTGGCATGTAAGATGGCTCTGGAA
CTCCTCACCCAAGAGTTTGGCATTCCCATTGAAAGACTTTATGTTACTTACTTTGGCGGG
GATGAAGCAGCTGGCTTAGAAGCAGATCTGGAATGCAAACAGATCTGGCAAAATTTGGGG
CTGGATGACACCAAAATCCTCCCAGGCAACATGAAGGATAACTTCTGGGAGATGGGTGAC
ACGGGCCCCTGTGGTCCTTGCAGTGAGATCCACTACGACCGGATTGGTGGTCGGGACGCC
GCACATCTTGTCAACCAGGACGACCCTAATGTGCTGGAGATCTGGAACCTTGTGTTCATC
CAGTATAACAGGGAAGCTGATGGCATTCTGAAACCTCTTCCCAAGAAAAGCATTGACACA
GGGATGGGCCTGGAACGACTGGTATCTGTGCTGCAGAATAAGATGTCCAACTATGACACT
GACCTTTTTGTCCCTTACTTTGAAGCCATTCAGAAGGGCACAGGTGCCCGACCATACACT
GGGAAAGTTGGTGCTGAGGATGCCGATGGGATTGACATGGCCTACCGGGTGCTGGCTGAC
CACGCTCGGACCATCACTGTGGCACTGGCTGATGGTGGCCGGCCTGACAACACAGGGCGT
GGATATGTGTTGAGACGGATTCTCCGCCGAGCTGTCCGATACGCCCATGAAAAGCTCAAT
GCCAGCAGGGGCTTCTTTGCTACGTTAGTGGATGTTGTCGTCCAGTCCCTGGGAGATGCA
TTTCCTGAGCTGAAGAAGGACCCAGACATGGTGAAGGACATCATTAATGAAGAAGAGGTG
CAGTTTCTCAAGACTCTCAGCAGAGGGCGTCGCATCCTGGACAGGAAAATTCAGAGCCTG
GGAGACAGCAAGACCATTCCCGGAGACACTGCTTGGCTCCTCTATGACACCTATGGGTTT
CCAGTGGATCTGACTGGACTGATTGCTGAAGAGAAGGGCCTGGTGGTAGACATGGATGGC
TTTGAAGAGGAGAGGAAACTGGCCCAGCTGAAATCACAGGGCAAGGGAGCTGGTGGGGAA
GACCTCATTATGCTGGACATTTACGCTATCGAAGAGCTCCGGGCACGGGGTCTGGAGGTC
ACAGATGATTCCCCAAAGTACAATTACCATTTGGACTCCAGTGGTAGCTATGTATTTGAG
AACACAGTGGCTACGGTGATGGCTCTGCGCAGGGAGAAGATGTTCGTGGAAGAGGTGTCC
ACAGGCCAGGAGTGTGGAGTGGTGCTGGACAAGACCTGTTTCTATGCTGAGCAAGGAGGC
CAGATCTATGACGAAGGCTACCTGGTGAAGGTGGATGACAGCAGTGAAGATAAAACAGAG
TTTACAGTGAAGAATGCTCAGGTCCGAGGAGGGTATGTGCTACACATTGGAACCATCTAC
GGTGACCTGAAAGTGGGGGATCAGGTCTGGCTGTTTATTGATGAGCCCCGACGAAGACCC
ATCATGAGCAACCACACAGCTACGCACATTCTGAACTTCGCCCTGCGCTCAGTGCTTGGG
GAAGCTGACCAGAAAGGCTCATTGGTTGCTCCTGACCGCCTCAGATTTGACTTTACTGCC
AAGGGAGCCATGTCCACCCAACAGATCAAGAAGGCTGAAGAGATTGCTAATGAGATGATT
GAGGCAGCCAAGGCCGTCTATACCCAGGATTGCCCCCTGGCAGCAGCGAAAGCCATCCAG
GGCCTACGGGCTGTGTTTGATGAGACCTATCCTGACCCTGTGCGAGTCGTCTCCATTGGG
GTCCCGGTGTCCGAGTTGCTGGATGACCCCTCTGGGCCTGCTGGCTCCCTGACTTCTGTT
GAGTTCTGTGGGGGAACGCACCTGCGGAACTCGAGTCATGCAGGAGCTTTTGTGATCGTG
ACGGAAGAAGCCATTGCCAAGGGTATCCGGAGGATTGTGGCTGTCACAGGTGCCGAGGCC
CAGAAGGCCCTCAGGAAAGCAGAGAGCTTGAAGAAATGTCTCTCTGTCATGGAAGCCAAA
GTGAAGGCTCAGACTGCTCCAAACAAGGATGTGCAGAGGGAGATCGCTGACCTTGGAGAG
GCCCTGGCCACTGCAGTCATCCCCCAGTGGCAGAAGGATGAATTGCGGGAGACTCTCAAA
TCCCTAAAGAAGGTCATGGATGACTTGGACCGAGCCAGCAAAGCCGATGTCCAGAAACGA
GTGTTAGAGAAGACGAAGCAGTTCATCGACAGCAACCCCAACCAGCCTCTTGTCATCCTG
GAGATGGAGAGCGGCGCCTCAGCCAAGGCCCTGAATGAAGCCTTGAAGCTCTTCAAGATG
CACTCCCCTCAGACTTCTGCCATGCTCTTCACGGTGGACAATGAGGCTGGCAAGATCACG
TGCCTGTGTCAAGTTCCCCAGAATGCAGCCAATCGGGGCTTAAAAGCCAGCGAGTGGGTG
CAGCAGGTGTCAGGCTTGATGGACGGTAAAGGTGGTGGCAAGGATGTGTCTGCACAGGCC
ACAGGCAAGAACGTTGGCTGCCTGCAGGAGGCGCTGCAGCTGGCCACTTCCTTCGCCCAG
CTGCGCCTCGGGGATGTAAAGAACTGA
|
| Enzyme 3 GenBank Gene ID |
NM_001605.2  |
| Enzyme 3 GeneCard ID |
AARS  |
| Enzyme 3 GenAtlas ID |
AARS  |
| Enzyme 3 HGNC ID |
HGNC:20  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
16q22 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Shiba K, Ripmaster T, Suzuki N, Nichols R, Plotz P, Noda T, Schimmel P: Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition. Biochemistry. 1995 Aug 22;34(33):10340-9. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P: The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science. 2009 Aug 7;325(5941):744-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Latour P, Thauvin-Robinet C, Baudelet-Mery C, Soichot P, Cusin V, Faivre L, Locatelli MC, Mayencon M, Sarcey A, Broussolle E, Camu W, David A, Rousson R: A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease. Am J Hum Genet. 2010 Jan;86(1):77-82. Epub 2009 Dec 31. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6069 |
| Enzyme 4 Name |
Serine--pyruvate aminotransferase |
| Enzyme 4 Synonyms |
- SPT
- Alanine--glyoxylate aminotransferase
- AGT
|
| Enzyme 4 Gene Name |
AGXT |
| Enzyme 4 Protein Sequence |
>Serine--pyruvate aminotransferase
MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEI
KEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIG
ARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLL
LVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF
YLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHG
RLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLR
IGLLGCNATRENVDRVTEALRAALQHCPKKKL
|
| Enzyme 4 Number of Residues |
392 |
| Enzyme 4 Molecular Weight |
43009.5 |
| Enzyme 4 Theoretical pI |
8.55 |
| Enzyme 4 GO Classification |
| Function |
| — |
| Process |
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in metabolic process |
| Enzyme 4 Specific Function |
L-serine + pyruvate = 3-hydroxypyruvate + L- alanine |
| Enzyme 4 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 4 Reactions |
- L-serine + pyruvate = 3-hydroxypyruvate + L-alanine [RN:R00585]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
36582  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P21549  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SPYA_HUMAN  |
| Enzyme 4 PDB ID |
1H0C  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1179 bp
ATGGCCTCTCACAAGCTGCTGGTGACCCCCCCCAAGGCCCTGCTCAAGCCCCTCTCCATC
CCCAACCAGCTCCTGCTGGGGCCTGGTCCTTCCAACCTGCCTCCTCGCATCATGGCAGCC
GGGGGGCTGCAGATGATCGGGTCCATGAGCAAGGATATGTACCAGATCATGGACGAGATC
AAGGAAGGCATCCAGTACGTGTTCCAGACCAGGAACCCACTCACACTGGTCATCTCTGGC
TCGGGACACTGTGCCCTGGAGGCCGCCCTGGTCAATGTGCTGGAGCCTGGGGACTCCTTC
CTGGTTGGGGCCAATGGCATTTGGGGGCAGCGAGCCGTGGACATCGGGGAGCGCATAGGA
GCCCGAGTGCACCCGATGACCAAGGACCCTGGAGGCCACTACACACTGCAGGAGGTGGAG
GAGGGCCTGGCCCAGCACAAGCCAGTGCTGCTGTTCTTAACCCACGGGGAGTCGTCCACC
GGCGTGCTGCAGCCCCTTGATGGCTTCGGGGAACTCTGCCACAGGTACAAGTGCCTGCTC
CTGGTGGATTCGGTGGCATCCCTGGGCGGGACCCCCCTTTACATGGACCGGCAAGGCATC
GACATCCTGTACTCGGGCTCCCAGAAGGCCCTGAACGCCCCTCCAGGGACCTCGCTCATC
TCCTTCAGTGACAAGGCCAAAAAGAAGATGTACTCCCGCAAGACGAAGCCCTTCTCCTTC
TACCTGGACATCAAGTGGCTGGCCAACTTCTGGGGCTGTGACGACCAGCCCAGGATGTAC
CATCACACAATCCCCGTCATCAGCCTGTACAGCCTGAGAGAGAGCCTGGCCCTCATTGCG
GAACAGGGCCTGGAGAACAGCTGGCGCCAGCACCGCGAGGCCGCGGCGTATCTGCATGGG
CGCCTGCAGGCACTGGGGCTGCAGCTCTTCGTGAAGGACCCGGCGCTCCGGCTTCCCACA
GTCACCACTGTGGCTGTACCCGCTGGCTATGACTGGAGAGACATCGTCAGCTACGTCATA
GACCACTTCGACATTGAGATCATGGGTGGCCTTGGGCCCTCCACGGGGAAGGTGCTGCGG
ATCGGCCTGCTGGGCTGCAATGCCACCCGCGAGAATGTGGACCGCGTGACGGAGGCCCTG
AGGGCGGCCCTGCAGCACTGCCCCAAGAAGAAGCTGTGA
|
| Enzyme 4 GenBank Gene ID |
X56092  |
| Enzyme 4 GeneCard ID |
AGXT  |
| Enzyme 4 GenAtlas ID |
AGXT  |
| Enzyme 4 HGNC ID |
HGNC:341  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
2q37.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Nishiyama K, Berstein G, Oda T, Ichiyama A: Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. Eur J Biochem. 1990 Nov 26;194(1):9-18. [PubMed
]
- Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J Cell Biol. 1990 Dec;111(6 Pt 1):2341-51. [PubMed
]
- Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ: Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem J. 1990 Jun 1;268(2):517-20. [PubMed
]
- Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ: Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. Genomics. 1991 May;10(1):34-42. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ: Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1. J Mol Biol. 2003 Aug 15;331(3):643-52. [PubMed
]
- Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A: Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. Biochem Biophys Res Commun. 1991 May 15;176(3):1093-9. [PubMed
]
- Purdue PE, Lumb MJ, Allsop J, Minatogawa Y, Danpure CJ: A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Genomics. 1992 May;13(1):215-8. [PubMed
]
- Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R: A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet. 1992 Nov;1(8):643-4. [PubMed
]
- Danpure CJ, Purdue PE, Fryer P, Griffiths S, Allsop J, Lumb MJ, Guttridge KM, Jennings PR, Scheinman JI, Mauer SM, et al.: Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. Am J Hum Genet. 1993 Aug;53(2):417-32. [PubMed
]
- Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. Biochimie. 1993;75(3-4):309-15. [PubMed
]
- von Schnakenburg C, Rumsby G: Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. J Med Genet. 1997 Jun;34(6):489-92. [PubMed
]
- von Schnakenburg C, Rumsby G: Identification of new mutations in primary hyperoxaluria type 1 (PH1). J Nephrol. 1998 Mar-Apr;11 Suppl 1:15-7. [PubMed
]
- Amoroso A, Pirulli D, Puzzer D, Ferri L, Crovella S, Ferrettini C, Marangella M, Mazzola G, Florian F: Gene symbol: AGXT. Disease: primary hyperoxaluria type I. Hum Genet. 1999 May;104(5):441. [PubMed
]
- Pirulli D, Puzzer D, Ferri L, Crovella S, Amoroso A, Ferrettini C, Marangella M, Mazzola G, Florian F: Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene. Hum Genet. 1999 Jun;104(6):523-5. [PubMed
]
- Rinat C, Wanders RJ, Drukker A, Halle D, Frishberg Y: Primary hyperoxaluria type I: a model for multiple mutations in a monogenic disease within a distinct ethnic group. J Am Soc Nephrol. 1999 Nov;10(11):2352-8. [PubMed
]
- Basmaison O, Rolland MO, Cochat P, Bozon D: Identification of 5 novel mutations in the AGXT gene. Hum Mutat. 2000 Jun;15(6):577. [PubMed
]
- Lumb MJ, Danpure CJ: Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. J Biol Chem. 2000 Nov 17;275(46):36415-22. [PubMed
]
- Coulter-Mackie MB, Tung A, Henderson HE, Toone JR, Applegarth DA: The AGT gene in Africa: a distinctive minor allele haplotype, a polymorphism (V326I), and a novel PH1 mutation (A112D) in Black Africans. Mol Genet Metab. 2003 Jan;78(1):44-50. [PubMed
]
- Santana A, Salido E, Torres A, Shapiro LJ: Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase. Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7277-82. Epub 2003 May 30. [PubMed
]
- van Woerden CS, Groothoff JW, Wijburg FA, Annink C, Wanders RJ, Waterham HR: Clinical implications of mutation analysis in primary hyperoxaluria type 1. Kidney Int. 2004 Aug;66(2):746-52. [PubMed
]
- Monico CG, Olson JB, Milliner DS: Implications of genotype and enzyme phenotype in pyridoxine response of patients with type I primary hyperoxaluria. Am J Nephrol. 2005 Mar-Apr;25(2):183-8. Epub 2005 Apr 21. [PubMed
]
- Frishberg Y, Rinat C, Shalata A, Khatib I, Feinstein S, Becker-Cohen R, Weismann I, Wanders RJ, Rumsby G, Roels F, Mandel H: Intra-familial clinical heterogeneity: absence of genotype-phenotype correlation in primary hyperoxaluria type 1 in Israel. Am J Nephrol. 2005 May-Jun;25(3):269-75. Epub 2005 Jun 15. [PubMed
]
- Coulter-Mackie MB, Lian Q, Applegarth D, Toone J: The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1. Mol Genet Metab. 2005 Sep-Oct;86(1-2):172-8. Epub 2005 Jun 15. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6131 |
| Enzyme 5 Name |
Alanine aminotransferase 1 |
| Enzyme 5 Synonyms |
- ALT1
- Glutamate pyruvate transaminase 1
- GPT 1
- Glutamic--alanine transaminase 1
- Glutamic--pyruvic transaminase 1
|
| Enzyme 5 Gene Name |
GPT |
| Enzyme 5 Protein Sequence |
>Alanine aminotransferase 1
MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPF
TEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSL
GAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRT
GVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVI
NPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPY
AGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDL
VVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQL
PPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLL
LEKLSRFHAKFTLEYS
|
| Enzyme 5 Number of Residues |
496 |
| Enzyme 5 Molecular Weight |
54636.4 |
| Enzyme 5 Theoretical pI |
7.20 |
| Enzyme 5 GO Classification |
| Function |
- 1-aminocyclopropane-1-carboxylate synthase activity
- binding
- carbon-sulfur lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in 1-aminocyclopropane-1-carboxylate synthase activity |
| Enzyme 5 Specific Function |
Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- L-alanine + 2-oxoglutarate = pyruvate + L-glutamate [RN:R00258]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P24298  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
ALAT1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1491 bp
ATGGCCTCGAGCACAGGTGACCGGAGCCAGGCGGTGAGGCATGGACTGAGGGCGAAGGTG
CTGACGCTGGACGGCATGAACCCGCGTGTGCGGAGAGTGGAGTACGCAGTGCGTGGCCCC
ATAGTGCAGCGAGCCTTGGAGCTGGAGCAGGAGCTGCGCCAGGGTGTGAAGAAGCCTTTC
ACCGAGGTCATCCGTGCCAACATCGGGGACGCACAGGCTATGGGGCAGAGGCCCATCACC
TTCCTGCGCCAGGTCTTGGCCCTCTGTGTTAACCCTGATCTTCTGAGCAGCCCCAACTTC
CCTGACGATGCCAAGAAAAGGGCGGAGCGCATCTTGCAGGCGTGTGGGGGCCACAGTCTG
GGGGCCTACAGCGTCAGCTCCGGCATCCAGCTGATCCGGGAGGACGTGGCGCGGTACATT
GAGAGGCGTGACGGAGGCATCCCTGCGGACCCCAACAACGTCTTCCTGTCCACAGGGGCC
AGCGATGCCATCGTGACGGTGCTGAAGCTGCTGGTGGCCGGCGAGGGCCACACACGCACG
GGTGTGCTCATCCCCATCCCCCAGTACCCACTCTACTCGGCCACGCTGGCAGAGCTGGGC
GCAGTGCAGGTGGATTACTACCTGGACGAGGAGCGTGCCTGGGCGCTGGACGTGGCCGAG
CTTCACCGTGCACTGGGCCAGGCGCGTGACCACTGCCGCCCTCGTGCGCTCTGTGTCATC
AACCCTGGCAACCCCACCGGGCAGGTGCAGACCCGCGAGTGCATCGAGGCCGTGATCCGC
TTCGCCTTCGAAGAGCGGCTCTTTCTGCTGGCGGACGAGGTGTACCAGGACAACGTGTAC
GCCGCGGGTTCGCAGTTCCACTCATTCAAGAAGGTGCTCATGGAGATGGGGCCGCCCTAC
GCCGGGCAGCAGGAGCTTGCCTCCTTCCACTCCACCTCCAAGGGCTACATGGGCGAGTGC
GGGTTCCGCGGCGGCTATGTGGAGGTGGTGAACATGGACGCTGCAGTGCAGCAGCAGATG
CTGAAGCTGATGAGTGTGCGGCTGTGCCCGCCGGTGCCAGGACAGGCCCTGCTGGACCTG
GTGGTCAGCCCGCCCGCGCCCACCGACCCCTCCTTTGCGCAGTTCCAGGCTGAGAAGCAG
GCAGTGCTGGCAGAGCTGGCGGCCAAGGCCAAGCTCACCGAGCAGGTCTTCAATGAGGCT
CCTGGCATCAGCTGCAACCCAGTGCAGGGCGCCATGTACTCCTTCCCGCGCGTGCAGCTG
CCCCCGCGGGCGGTGGAGCGCGCTCAGGAGCTGGGCCTGGCCCCCGATATGTTCTTCTGC
CTGCGCCTCCTGGAGGAGACCGGCATCTGCGTGGTGCCAGGGAGCGGCTTTGGGCAGCGG
GAAGGCACCTACCACTTCCGGATGACCATTCTGCCCCCCTTGGAGAAACTGCGGCTGCTG
CTGGAGAAGCTGAGCAGGTTCCATGCCAAGTTCACCCTCGAGTACTCCTAG
|
| Enzyme 5 GenBank Gene ID |
BT006992  |
| Enzyme 5 GeneCard ID |
GPT  |
| Enzyme 5 GenAtlas ID |
GPT  |
| Enzyme 5 HGNC ID |
HGNC:4552  |
| Enzyme 5 Chromosome Location |
8 |
| Enzyme 5 Locus |
8q24.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Sohocki MM, Sullivan LS, Harrison WR, Sodergren EJ, Elder FF, Weinstock G, Tanase S, Daiger SP: Human glutamate pyruvate transaminase (GPT): localization to 8q24.3, cDNA and genomic sequences, and polymorphic sites. Genomics. 1997 Mar 1;40(2):247-52. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ishiguro M, Takio K, Suzuki M, Oyama R, Matsuzawa T, Titani K: Complete amino acid sequence of human liver cytosolic alanine aminotransferase (GPT) determined by a combination of conventional and mass spectral methods. Biochemistry. 1991 Oct 29;30(43):10451-7. [PubMed
]
- Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
7528 |
| Enzyme 6 Name |
Peptidoglycan recognition protein 1 |
| Enzyme 6 Synonyms |
- Peptidoglycan recognition protein short
- PGRP-S
|
| Enzyme 6 Gene Name |
PGLYRP1 |
| Enzyme 6 Protein Sequence |
>Peptidoglycan recognition protein 1
MSRRSMLLAWALPSLLRLGAAQETEDPACCSPIVPRNEWKALASECAQHLSLPLRYVVVS
HTAGSSCNTPASCQQQARNVQHYHMKTLGWCDVGYNFLIGEDGLVYEGRGWNFTGAHSGH
LWNPMSIGISFMGNYMDRVPTPQAIRAAQGLLACGVAQGALRSNYVLKGHRDVQRTLSPG
NQLYHLIQNWPHYRSP
|
| Enzyme 6 Number of Residues |
196 |
| Enzyme 6 Molecular Weight |
21730.6 |
| Enzyme 6 Theoretical pI |
8.68 |
| Enzyme 6 GO Classification |
| Function |
- N-acetylmuramoyl-L-alanine amidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
- protein binding
|
| Process |
- aminoglycan metabolic process
- carbohydrate metabolic process
- glycosaminoglycan metabolic process
- metabolic process
- peptidoglycan catabolic process
- peptidoglycan metabolic process
- polysaccharide metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in N-acetylmuramoyl-L-alanine amidase activity |
| Enzyme 6 Specific Function |
Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
5042404  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
O75594  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PGRP1_HUMAN  |
| Enzyme 6 PDB ID |
1YCK  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>591 bp
ATGTCCCGCCGCTCTATGCTGCTTGCCTGGGCTCTCCCCAGCCTCCTTCGACTCGGAGCG
GCTCAGGAGACAGAAGACCCGGCCTGCTGCAGCCCCATAGTGCCCCGGAACGAGTGGAAG
GCCCTGGCATCAGAGTGCGCCCAGCACCTGAGCCTGCCCTTACGCTATGTGGTGGTATCG
CACACGGCGGGCAGCAGCTGCAACACCCCCGCCTCGTGCCAGCAGCAGGCCCGGAATGTG
CAGCACTACCACATGAAGACACTGGGCTGGTGCGACGTGGGCTACAACTTCCTGATTGGA
GAAGACGGGCTCGTATACGAGGGCCGTGGCTGGAACTTCACGGGTGCCCACTCAGGTCAC
TTATGGAACCCCATGTCCATTGGCATCAGCTTCATGGGCAACTACATGGATCGGGTGCCC
ACACCCCAGGCCATCCGGGCAGCCCAGGGTCTACTGGCCTGCGGTGTGGCTCAGGGAGCC
CTGAGGTCCAACTATGTGCTCAAAGGACACCGGGATGTGCAGCGTACACTCTCTCCAGGC
AACCAGCTCTACCACCTCATCCAGAATTGGCCACACTACCGCTCCCCCTGA
|
| Enzyme 6 GenBank Gene ID |
AC007785  |
| Enzyme 6 GeneCard ID |
PGLYRP1  |
| Enzyme 6 GenAtlas ID |
PGLYRP1  |
| Enzyme 6 HGNC ID |
HGNC:8904  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
19q13.2-q13.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Kang D, Liu G, Lundstrom A, Gelius E, Steiner H: A peptidoglycan recognition protein in innate immunity conserved from insects to humans. Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):10078-82. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Liu C, Xu Z, Gupta D, Dziarski R: Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules. J Biol Chem. 2001 Sep 14;276(37):34686-94. Epub 2001 Jul 18. [PubMed
]
- Lu X, Wang M, Qi J, Wang H, Li X, Gupta D, Dziarski R: Peptidoglycan recognition proteins are a new class of human bactericidal proteins. J Biol Chem. 2006 Mar 3;281(9):5895-907. Epub 2005 Dec 14. [PubMed
]
- Guan R, Wang Q, Sundberg EJ, Mariuzza RA: Crystal structure of human peptidoglycan recognition protein S (PGRP-S) at 1.70 A resolution. J Mol Biol. 2005 Apr 8;347(4):683-91. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
7884 |
| Enzyme 7 Name |
Large neutral amino acids transporter small subunit 2 |
| Enzyme 7 Synonyms |
- L-type amino acid transporter 2
- hLAT2
- Solute carrier family 7 member 8
|
| Enzyme 7 Gene Name |
SLC7A8 |
| Enzyme 7 Protein Sequence |
>Large neutral amino acids transporter small subunit 2
MEEGARHRNNTEKKHPGGGESDASPEAGSGGGGVALKKEIGLVSACGIIVGNIIGSGIFV
SPKGVLENAGSVGLALIVWIVTGFITVVGALCYAELGVTIPKSGGDYSYVKDIFGGLAGF
LRLWIAVLVIYPTNQAVIALTFSNYVLQPLFPTCFPPESGLRLLAAICLLLLTWVNCSSV
RWATRVQDIFTAGKLLALALIIIMGIVQICKGEYFWLEPKNAFENFQEPDIGLVALAFLQ
GSFAYGGWNFLNYVTEELVDPYKNLPRAIFISIPLVTFVYVFANVAYVTAMSPQELLASN
AVAVTFGEKLLGVMAWIMPISVALSTFGGVNGSLFTSSRLFFAGAREGHLPSVLAMIHVK
RCTPIPALLFTCISTLLMLVTSDMYTLINYVGFINYLFYGVTVAGQIVLRWKKPDIPRPI
KINLLFPIIYLLFWAFLLVFSLWSEPVVCGIGLAIMLTGVPVYFLGVYWQHKPKCFSDFI
ELLTLVSQKMCVVVYPEVERGSGTEEANEDMEEQQQPMYQPTPTKDKDVAGQPQP
|
| Enzyme 7 Number of Residues |
535 |
| Enzyme 7 Molecular Weight |
58381.1 |
| Enzyme 7 Theoretical pI |
5.75 |
| Enzyme 7 GO Classification |
| Function |
- active transmembrane transporter activity
- amine transmembrane transporter activity
- amino acid transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- amine transport
- amino acid transport
- establishment of localization
- transmembrane transport
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 7 General Function |
Involved in transport |
| Enzyme 7 Specific Function |
Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
- 40-60
72-92
113-133
155-175
189-209
231-251
268-288
310-330
362-382
388-408
424-444
447-467
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
12597192  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9UHI5  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
LAT2_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1608 bp
ATGGAAGAAGGAGCCAGGCACCGAAACAACACCGAAAAGAAACACCCAGGTGGGGGCGAG
TCGGACGCCAGCCCCGAGGCTGGTTCCGGAGGGGGCGGAGTAGCCCTGAAGAAAGAGATC
GGATTGGTCAGTGCCTGTGGTATCATCGTAGGGAACATCATCGGCTCTGGAATCTTTGTC
TCGCCAAAGGGAGTGCTGGAGAATGCTGGTTCTGTGGGCCTTGCTCTCATCGTCTGGATT
GTGACGGGCTTCATCACAGTTGTGGGAGCCCTCTGCTATGCTGAACTCGGGGTCACCATC
CCCAAATCTGGAGGTGACTACTCCTATGTCAAGGACATCTTCGGAGGACTGGCTGGGTTC
CTGAGGCTGTGGATTGCTGTGCTGGTGATCTACCCCACCAACCAGGCTGTCATCGCCCTC
ACCTTCTCCAACTACGTGCTGCAGCCGCTCTTCCCCACCTGCTTCCCCCCAGAGTCTGGC
CTTCGGCTCCTGGCTGCCATCTGCTTATTGCTCCTCACATGGGTCAACTGTTCCAGTGTG
CGGTGGGCCACCCGGGTTCAAGACATCTTCACAGCTGGGAAGCTCCTGGCCTTGGCCCTG
ATTATCATCATGGGGATTGTACAGATATGCAAAGGAGAGTACTTCTGGCTGGAGCCAAAG
AATGCATTTGAGAATTTCCAGGAACCTGACATCGGCCTCGTCGCACTGGCTTTCCTTCAG
GGCTCCTTTGCCTATGGAGGCTGGAACTTTCTGAATTACGTGACTGAGGAGCTTGTTGAT
CCCTACAAGAACCTTCCCAGAGCCATCTTCATCTCCATCCCACTGGTCACATTTGTGTAT
GTCTTTGCCAATGTCGCTTATGTCACTGCAATGTCCCCCCAGGAGCTGCTGGCATCCAAC
GCCGTCGCTGTGACTTTTGGAGAGAAGCTCCTAGGAGTCATGGCCTGGATCATGCCCATT
TCTGTTGCCCTGTCCACATTTGGAGGAGTTAATGGGTCTCTCTTCACCTCCTCTCGGCTG
TTCTTCGCTGGAGCCCGAGAGGGCCACCTTCCCAGTGTGTTGGCCATGATCCACGTGAAG
CGCTGCACCCCAATCCCAGCCCTGCTCTTCACATGCATCTCCACCCTGCTGATGCTGGTC
ACCAGCGACATGTACACACTCATCAACTACGTGGGCTTCATCAACTACCTCTTCTATGGG
GTCACGGTTGCTGGACAGATAGTCCTTCGCTGGAAGAAGCCTGATATCCCCCGCCCCATC
AAGATCAACCTGCTGTTCCCCATCATCTACTTGCTGTTCTGGGCCTTCCTGCTGGTCTTC
AGCCTGTGGTCAGAGCCGGTGGTGTGTGGCATTGGCCTGGCCATCATGCTGACAGGAGTG
CCTGTCTATTTCCTGGGTGTTTACTGGCAACACAAGCCCAAGTGTTTCAGTGACTTCATT
GAGCTGCTAACCCTGGTGAGCCAGAAGATGTGTGTGGTCGTGTACCCCGAGGTGGAGCGG
GGCTCAGGGACAGAGGAGGCTAATGAGGACATGGAGGAGCAGCAGCAGCCCATGTACCAA
CCCACTCCCACGAAGGACAAGGACGTGGCGGGGCAGCCCCAGCCCTGA
|
| Enzyme 7 GenBank Gene ID |
AB037669  |
| Enzyme 7 GeneCard ID |
SLC7A8  |
| Enzyme 7 GenAtlas ID |
SLC7A8  |
| Enzyme 7 HGNC ID |
HGNC:11066  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
14q11.2 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Pineda M, Fernandez E, Torrents D, Estevez R, Lopez C, Camps M, Lloberas J, Zorzano A, Palacin M: Identification of a membrane protein, LAT-2, that Co-expresses with 4F2 heavy chain, an L-type amino acid transport activity with broad specificity for small and large zwitterionic amino acids. J Biol Chem. 1999 Jul 9;274(28):19738-44. [PubMed
]
- Rossier G, Meier C, Bauch C, Summa V, Sordat B, Verrey F, Kuhn LC: LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine. J Biol Chem. 1999 Dec 3;274(49):34948-54. [PubMed
]
- Borsani G, Bassi MT, Sperandeo MP, De Grandi A, Buoninconti A, Riboni M, Manzoni M, Incerti B, Pepe A, Andria G, Ballabio A, Sebastio G: SLC7A7, encoding a putative permease-related protein, is mutated in patients with lysinuric protein intolerance. Nat Genet. 1999 Mar;21(3):297-301. [PubMed
]
- Park SY, Kim JK, Kim IJ, Choi BK, Jung KY, Lee S, Park KJ, Chairoungdua A, Kanai Y, Endou H, Kim DK: Reabsorption of neutral amino acids mediated by amino acid transporter LAT2 and TAT1 in the basolateral membrane of proximal tubule. Arch Pharm Res. 2005 Apr;28(4):421-32. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Broer A, Friedrich B, Wagner CA, Fillon S, Ganapathy V, Lang F, Broer S: Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains. Biochem J. 2001 May 1;355(Pt 3):725-31. [PubMed
]
- Simmons-Willis TA, Koh AS, Clarkson TW, Ballatori N: Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2. Biochem J. 2002 Oct 1;367(Pt 1):239-46. [PubMed
]
- Liu X, Charrier L, Gewirtz A, Sitaraman S, Merlin D: CD98 and intracellular adhesion molecule I regulate the activity of amino acid transporter LAT-2 in polarized intestinal epithelia. J Biol Chem. 2003 Jun 27;278(26):23672-7. Epub 2003 Apr 25. [PubMed
]
- Gandhi MD, Pal D, Mitra AK: Identification and functional characterization of a Na(+)-independent large neutral amino acid transporter (LAT2) on ARPE-19 cells. Int J Pharm. 2004 May 4;275(1-2):189-200. [PubMed
]
- Fraga S, Pinho MJ, Soares-da-Silva P: Expression of LAT1 and LAT2 amino acid transporters in human and rat intestinal epithelial cells. Amino Acids. 2005 Nov;29(3):229-33. Epub 2005 Jul 20. [PubMed
]
- Li S, Whorton AR: Identification of stereoselective transporters for S-nitroso-L-cysteine: role of LAT1 and LAT2 in biological activity of S-nitrosothiols. J Biol Chem. 2005 May 20;280(20):20102-10. Epub 2005 Mar 15. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
8009 |
| Enzyme 8 Name |
Cysteine desulfurase, mitochondrial |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
NFS1 |
| Enzyme 8 Protein Sequence |
>Cysteine desulfurase, mitochondrial
MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLY
MDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPRE
IIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQK
SGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKI
PLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPL
VVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAY
VEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD
YTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH
|
| Enzyme 8 Number of Residues |
457 |
| Enzyme 8 Molecular Weight |
50195.2 |
| Enzyme 8 Theoretical pI |
8.45 |
| Enzyme 8 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- cysteine desulfurase activity
- pyridoxal phosphate binding
- sulfurtransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- cysteine metabolic process
- metabolic process
- sulfur amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in metabolic process |
| Enzyme 8 Specific Function |
Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
- L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine [RN:R07460]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
24042327  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9Y697  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
NFS1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1374 bp
ATGCTGCTCCGAGTCGCTTGGAGGCGGGCGGCAGTGGCGGTGACAGCGGCTCCAGGGCCG
AAGCCCGCGGCGCCCACTCGGGGGCTGCGCCTGCGCGTTGGAGACCGTGCTCCTCAGTCT
GCGGTTCCCGCAGATACAACCGCTGCCCCGGAGGTGGGGCCAGTGCTGCGACCTCTCTAT
ATGGATGTGCAAGCTACAACTCCTCTGGACCCCCGGGTGCTTGATGCCATGCTCCCTTAC
CTAATCAACTACTATGGGAACCCACACTCCCGGACACATGCTTATGGCTGGGAGAGTGAG
GCAGCCATGGAACGTGCTCGTCAGCAAGTAGCATCTCTGATTGGAGCTGATCCTCGTGAG
ATCATTTTTACTAGTGGTGCTACTGAATCCAACAACATAGCAATTAAGGGGGTGGCCCGA
TTCTACAGGTCACGGAAAAAGCACTTGATCACCACCCAGACAGAACACAAATGTGTCTTG
GACTCCTGCCGTTCACTGGAAGCTGAGGGCTTTCAGGTCACCTACCTCCCAGTGCAGAAG
AGTGGGATCATTGACCTAAAGGAACTAGAGGCTGCTATCCAGCCAGATACTAGCCTGGTG
TCAGTCATGACTGTGAACAATGAGATTGGAGTGAAGCAGCCTATTGCAGAAATAGGGCGG
ATTTGCAGTTCCAGAAAGGTATATTTCCATACTGATGCAGCCCAGGCTGTTGGAAAAATC
CCACTTGATGTCAATGACATGAAAATTGATCTCATGAGCATTAGTGGTCACAAAATCTAC
GGTCCCAAAGGGGTTGGTGCCATCTACATCCGTCGCCGGCCCCGTGTGCGTGTGGAGGCC
CTGCAGAGTGGAGGGGGGCAGGAGCGGGGTATGCGGTCTGGGACAGTGCCCACACCCTTA
GTGGTGGGGTTGGGGGCTGCGTGTGAGGTGGCACAGCAAGAGATGGAGTATGACCACAAG
CGAATCTCAAAGTTGTCAGAGCGGCTGATACAGAATATAATGAAGAGCCTTCCAGATGTG
GTGATGAATGGGGACCCTAAGCACCATTATCCCGGCTGTATCAACCTCTCCTTTGCATAT
GTGGAAGGGGAAAGTCTGCTGATGGCACTGAAGGACGTTGCCTTATCCTCAGGGAGTGCC
TGCACCTCTGCATCCCTGGAGCCCTCTTATGTGCTTAGAGCAATTGGCACTGATGAGGAT
TTAGCGCACTCTTCTATCAGGTTTGGAATTGGCGCTTTCACTACAGAGGAGGAAGTGGAC
TACACAGTGGAGAAATGCATTCAGCATGTGAATCGTCTTCGAGAAATGAGCCCTCTCTGG
GAGATGGTTCAGGATGGCATTGACCTCAAGAGCATCAAGTGGACCCAACACTAG
|
| Enzyme 8 GenBank Gene ID |
AF097025  |
| Enzyme 8 GeneCard ID |
NFS1  |
| Enzyme 8 GenAtlas ID |
NFS1  |
| Enzyme 8 HGNC ID |
HGNC:15910  |
| Enzyme 8 Chromosome Location |
2 |
| Enzyme 8 Locus |
20q11.22 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Land T, Rouault TA: Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol Cell. 1998 Dec;2(6):807-15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G: Characterization of 16 novel human genes showing high similarity to yeast sequences. Yeast. 2001 Jan 15;18(1):69-80. [PubMed
]
- Tong WH, Rouault T: Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 2000 Nov 1;19(21):5692-700. [PubMed
]
- Marelja Z, Stocklein W, Nimtz M, Leimkuhler S: A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. J Biol Chem. 2008 Sep 12;283(37):25178-85. Epub 2008 Jul 23. [PubMed
]
- Shi Y, Ghosh MC, Tong WH, Rouault TA: Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis. Hum Mol Genet. 2009 Aug 15;18(16):3014-25. Epub 2009 May 18. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
8562 |
| Enzyme 9 Name |
Sodium-coupled neutral amino acid transporter 3 |
| Enzyme 9 Synonyms |
- N-system amino acid transporter 1
- Na(+)-coupled neutral amino acid transporter 3
- Solute carrier family 38 member 3
- System N amino acid transporter 1
|
| Enzyme 9 Gene Name |
SLC38A3 |
| Enzyme 9 Protein Sequence |
>Sodium-coupled neutral amino acid transporter 3
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
|
| Enzyme 9 Number of Residues |
504 |
| Enzyme 9 Molecular Weight |
55772.4 |
| Enzyme 9 Theoretical pI |
8.01 |
| Enzyme 9 GO Classification |
Not Available |
| Enzyme 9 General Function |
Amino acid transport and metabolism |
| Enzyme 9 Specific Function |
Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
- 83-103
106-126
144-164
187-207
213-233
324-344
366-386
408-428
431-451
471-491
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
5870893  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q99624  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
S38A3_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1515 bp
ATGGAGGCGCCTTTGCAGACAGAGATGGTGGAGCTGGTGCCCAATGGCAAACACTCAGAG
GGGCTGCTCCCGGTCATCACCCCCATGGCAGGCAACCAGAGGGTCGAGGACCCTGCACGG
AGCTGTATGGAGGGCAAGAGCTTCCTACAGAAAAGTCCCAGCAAGGAGCCACACTTCACT
GACTTCGAGGGGAAGACATCATTCGGGATGTCAGTGTTCAACCTCAGCAATGCCATCATG
GGCAGCGGCATCCTGGGACTCGCCTATGCCATGGCCAATACGGGCATTATCCTTTTCCTG
TTCCTGTTGACAGCTGTCGCCTTGCTCTCCAGCTACTCCATCCACCTGCTACTCAAGTCC
TCAGGGGTCGTGGGCATCCGTGCCTATGAGCAGCTGGGCTACCGTGCCTTTGGGACCCCA
GGAAAGCTGGCAGCAGCCCTGGCCATCACGCTCCAGAACATCGGAGCCATGTCCAGCTAC
CTGTACATCATCAAGTCTGAGCTGCCACTTGTCATACAGACCTTCCTGAACCTGGAGGAG
AAAACCTCGGACTGGTACATGAACGGGAACTACCTGGTAATCCTTGTCTCTGTCACCATC
ATTCTGCCCCTGGCACTGATGCGGCAGCTTGGCTACCTGGGCTACTCCAGCGGCTTCTCT
CTTAGCTGCATGGTGTTCTTCCTAATTGCAGTCATCTACAAAAAGTTCCACGTGCCCTGC
CCACTGCCCCCCAACTTCAACAACACCACAGGCAACTTCAGCCACGTGGAGATCGTGAAG
GAGAAGGTGCAGCTGCAGGTCGAGCCTGAGGCTTCAGCCTTCTGCACTCCCAGCTACTTC
ACGCTCAACTCACAGACAGCATACACCATCCCCATCATGGCCTTCGCCTTCGTCTGCCAC
CCCGAGGTGCTGCCCATCTATACTGAGCTCAAGGACCCCTCCAAGAAGAAGATGCAGCAC
ATCTCCAACCTGTCCATCGCTGTCATGTACATCATGTACTTCCTGGCTGCCCTCTTCGGC
TACCTCACCTTCTACAACGGGGTGGAGTCGGAGCTGCTGCACACCTACAGCAAGGTGGAC
CCGTTTGACGTCCTGATCCTGTGTGTGCGCGTGGCCGTGCTGACAGCAGTCACGCTCACA
GTGCCCATCGTTCTGTTCCCGGTGCGCCGCGCCATCCAGCAGATGCTGTTTCCAAACCAG
GAGTTCAGCTGGCTGCGGCATGTGCTTATTGCCGTTGGCCTGCTCACTTGTATCAACCTG
CTGGTCATCTTTGCCCCCAACATCCTGGGCATCTTTGGGGTCATCGGTGCCACATCTGCC
CCATTCCTCATCTTCATCTTCCCTGCCATCTTCTACTTCCGAATCATGCCCACGGAGAAG
GAGCCTGCAAGATCCACCCCCAAAATCCTGGCCCTGTGTTTTGCTATGCTTGGCTTCTTG
CTGATGACCATGAGCTTGAGCTTCATCATCATTGACTGGGCCTCAGGGACCAGCCGGCAT
GGAGGAAACCACTAG
|
| Enzyme 9 GenBank Gene ID |
NM_006841.4  |
| Enzyme 9 GeneCard ID |
SLC38A3  |
| Enzyme 9 GenAtlas ID |
SLC38A3  |
| Enzyme 9 HGNC ID |
HGNC:18044  |
| Enzyme 9 Chromosome Location |
3 |
| Enzyme 9 Locus |
3p21.3 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Fei YJ, Sugawara M, Nakanishi T, Huang W, Wang H, Prasad PD, Leibach FH, Ganapathy V: Primary structure, genomic organization, and functional and electrogenic characteristics of human system N 1, a Na+- and H+-coupled glutamine transporter. J Biol Chem. 2000 Aug 4;275(31):23707-17. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lerman MI, Minna JD: The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium. Cancer Res. 2000 Nov 1;60(21):6116-33. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
8650 |
| Enzyme 10 Name |
Neutral amino acid transporter A |
| Enzyme 10 Synonyms |
- Alanine/serine/cysteine/threonine transporter 1
- ASCT-1
- SATT
- Solute carrier family 1 member 4
|
| Enzyme 10 Gene Name |
SLC1A4 |
| Enzyme 10 Protein Sequence |
>Neutral amino acid transporter A
MEKSNETNGYLDSAQAGPAAGPGAPGTAAGRARRCAGFLRRQALVLLTVSGVLAGAGLGA
ALRGLSLSRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASCLGRLGGIAVAY
FGLTTLSASALAVALAFIIKPGSGAQTLQSSDLGLEDSGPPPVPKETVDSFLDLARNLFP
SNLVVAAFRTYATDYKVVTQNSSSGNVTHEKIPIGTEIEGMNILGLVLFALVLGVALKKL
GSEGEDLIRFFNSLNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFA
SILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSSSATLPSMMKCIEENN
GVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELNAGQIFTILVTATASSVGA
AGVPAGGVLTIAIILEAIGLPTHDLPLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQK
ATKKGEQELAEVKVEAIPNCKSEEETSPLVTHQNPAGPVASAPELESKESVL
|
| Enzyme 10 Number of Residues |
532 |
| Enzyme 10 Molecular Weight |
55722.5 |
| Enzyme 10 Theoretical pI |
6.18 |
| Enzyme 10 GO Classification |
| Function |
- carboxylic acid transmembrane transporter activity
- dicarboxylic acid transmembrane transporter activity
- organic acid transmembrane transporter activity
- sodium:dicarboxylate symporter activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- carboxylic acid transport
- dicarboxylic acid transport
- establishment of localization
- organic acid transport
- transport
|
| Component |
|
|
| Enzyme 10 General Function |
Involved in sodium:dicarboxylate symporter activity |
| Enzyme 10 Specific Function |
Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
- 42-62
88-108
119-139
217-237
257-277
298-318
328-348
373-393
418-438
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
62822396  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P43007  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
SATT_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1596 bp
ATGGCCCTGGGTGAAGAAAAGGCAGAAGCGGAAGCATCTGAAGACACAAAGGCCCAGTCC
TATGGGAGAGGGAGCTGCAGGGAGCGGGAGCTGGACATCCCAGGGCCCATGAGTGGGGAG
CAGCCCCCACGCCTGGAAGCTGAGGGAGGGCTCATCTCCCCTGTATGGGGGGCAGAAGGG
ATACCTGCCCCTACTTGCTGGATTGGGACTGACCCTGGCGGCCCCTCTAGAGCCCACCAG
CCACAGGCCAGTGATGCCAACAGAGAGCCCGTAGCTGAGAGGTCTGAGCCTGCACTCAGT
GGCCTGCCTCCTGCCACCATGGGGTCTGGAGACCTTCTGCTCTCCGGGGAAAGCCAGGTG
GAGAAGACCAAGCTTTCTTCCTCCGAGGAGTTCCCTCAGACTCTGAGCCTTCCCAGAACA
ACAACTATTTGCTCAGGACATGATGCTGATACCGAAGATGATCCATCCCTAGCAGATTTG
CCCCAGGCACTGGACCTCAGCCAGCAGCCTCACAGCTCAGGTCTCTCTTGCCTGTCACAG
TGGAAGTCCGTGCTGAGCCCAGGTTCCGCAGCTCAGCCTTCCAGCTGCAGCATCTCTGCT
TCCTCCACAGGCAGCAGTCTCCAGGGTCACCAGGAGAGGGCGGAGCCTCGTGGTGGTTCT
CTGGCCAAGGTCTCCTCCTCCCTGGAGCCGGTCGTCCCCCAGGAACCTTCCTCTGTGGTG
GGGCTAGGACCTCGGCCCCAGTGGTCACCACAGCCTGTGTTCTCTGGGGGTGATGCTTCT
GGGCTAGGCAGGAGACGCCTCTCCTTCCAGGCTGAGTACTGGGCCTGTGTGCTGCCAGAT
TCCCTGCCTCCATCACCCGACCGCCACTCCCCTCTCTGGAACCCAAATAAAGAGTATGAA
GATCTGCTTGACTATACTTACCCACTGAGGCCCGGGCCTCAGCTCCCAAAGCACCTTGAT
AGCCGTGTGCCAGCTGACCCTGTCCTGCAGGACTCCGGGGTAGACCTGGATAGCTTCTCT
GTCTCTCCAGCAAGCACCCTCAAATCACCTACTAATGTCTCCCCCAACTGCCCACCAGCA
GAGGCCACTGCCCTGCCATTTTCTGGGCCCAGAGAGCCAAGCCTTAAGCAGTGGCCCTCC
AGAGTACCCCAGAAACAGGGTGGCATGGGCTTGGCATCTTGGAGCCAACTTGCATCTACC
CCCAGAGCCCCAGGCAGTAGGGATGCTCGTTGGGAGCGCAGAGAGCCAGCCCTGAGGGGT
GCGAAGGACCGGCTGACTATAGGCAAGCACCTTGATATGGGCTCTCCCCAGCTAAGGACA
CGGGACAGAGGGTGGCCCTCGCCCAGGCCAGAGAGGGAGAAGAGGACCAGCCAGAGTGCC
CGGCGCCCTACCTGCACAGAGTCTAGGTGGAAATCAGAAGAGGAAGTGGAAAGTGATGAC
GAGTATCTTGCCCTCCCCGCTCGGCTGACACAGACATTTTGCTGTCAGCTGGAAGAGCTG
ATCTGCTGGCTGTATAATGTTGCAGATGTTACTGACCACGGGACTGCAGCCAGGTCCAAT
CTTACAAGTCTCAAGTCTTCTCTGCAGCTTTACCGG
|
| Enzyme 10 GenBank Gene ID |
AC007386  |
| Enzyme 10 GeneCard ID |
SLC1A4  |
| Enzyme 10 GenAtlas ID |
SLC1A4  |
| Enzyme 10 HGNC ID |
HGNC:10942  |
| Enzyme 10 Chromosome Location |
2 |
| Enzyme 10 Locus |
2p15-p13 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Arriza JL, Kavanaugh MP, Fairman WA, Wu YN, Murdoch GH, North RA, Amara SG: Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J Biol Chem. 1993 Jul 25;268(21):15329-32. [PubMed
]
- Shafqat S, Tamarappoo BK, Kilberg MS, Puranam RS, McNamara JO, Guadano-Ferraz A, Fremeau RT Jr: Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters. J Biol Chem. 1993 Jul 25;268(21):15351-5. [PubMed
]
- Hofmann K, Duker M, Fink T, Lichter P, Stoffel W: Human neutral amino acid transporter ASCT1: structure of the gene (SLC1A4) and localization to chromosome 2p13-p15. Genomics. 1994 Nov 1;24(1):20-6. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
9258 |
| Enzyme 11 Name |
Alanine aminotransferase 2 |
| Enzyme 11 Synonyms |
- ALT2
- Glutamate pyruvate transaminase 2
- GPT 2
- Glutamic--alanine transaminase 2
- Glutamic--pyruvic transaminase 2
|
| Enzyme 11 Gene Name |
GPT2 |
| Enzyme 11 Protein Sequence |
>Alanine aminotransferase 2
MQRAAALVRRGCGPRTPSSWGRSQSSAAAEASAVLKVRPERSRRERILTLESMNPQVKAV
EYAVRGPIVLKAGEIELELQRGIKKPFTEVIRANIGDAQAMGQQPITFLRQVMALCTYPN
LLDSPSFPEDAKKRARRILQACGGNSLGSYSASQGVNCIREDVAAYITRRDGGVPADPDN
IYLTTGASDGISTILKILVSGGGKSRTGVMIPIPQYPLYSAVISELDAIQVNYYLDEENC
WALNVNELRRAVQEAKDHCDPKVLCIINPGNPTGQVQSRKCIEDVIHFAWEEKLFLLADE
VYQDNVYSPDCRFHSFKKVLYEMGPEYSSNVELASFHSTSKGYMGECGYRGGYMEVINLH
PEIKGQLVKLLSVRLCPPVSGQAAMDIVVNPPVAGEESFEQFSREKESVLGNLAKKAKLT
EDLFNQVPGIHCNPLQGAMYAFPRIFIPAKAVEAAQAHQMAPDMFYCMKLLEETGICVVP
GSGFGQREGTYHFRMTILPPVEKLKTVLQKVKDFHINFLEKYA
|
| Enzyme 11 Number of Residues |
523 |
| Enzyme 11 Molecular Weight |
57903.1 |
| Enzyme 11 Theoretical pI |
7.77 |
| Enzyme 11 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 11 Specific Function |
Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- L-alanine + 2-oxoglutarate = pyruvate + L-glutamate [RN:R00258]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
19046894  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q8TD30  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
ALAT2_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1572 bp
ATGCAGCGGGCGGCGGCGCTGGTCCGGCGGGGCTGTGGTCCCCGGACCCCCAGCTCCTGG
GGCCGCAGCCAGAGCAGCGCGGCCGCCGAGGCCTCGGCGGTGCTCAAGGTGCGGCCCGAG
CGCAGCCGGCGCGAGCGCATCCTCACGCTGGAGTCCATGAACCCGCAGGTGAAGGCGGTG
GAGTACGCCGTGCGGGGACCCATCGTGCTCAAGGCCGGCGAGATCGAGCTCGAGCTGCAG
CGGGGTATCAAAAAGCCATTCACAGAGGTCATCCGAGCCAACATCGGGGACGCCCAGGCT
ATGGGGCAGCAGCCAATCACCTTCCTCCGGCAGGTGATGGCACTATGCACCTACCCAAAC
CTGCTGGACAGCCCCAGCTTCCCAGAAGATGCTAAGAAACGTGCCCGGCGGATCCTGCAG
GCTTGTGGCGGGAACAGCCTGGGGTCCTACAGTGCTAGCCAGGGTGTCAACTGCATCCGT
GAAGATGTGGCTGCCTACATCACCAGGAGGGATGGCGGTGTGCCTGCGGACCCCGACAAC
ATCTACCTGACCACGGGAGCTAGTGACGGCATTTCTACGATCCTGAAGATCCTCGTCTCC
GGGGGCGGCAAGTCACGGACAGGTGTGATGATCCCCATCCCACAATATCCCCTCTATTCA
GCTGTCATCTCTGAGCTCGACGCCATCCAGGTGAATTACTACCTGGACGAGGAGAACTGC
TGGGCGCTGAATGTGAATGAGCTCCGGCGGGCGGTGCAGGAGGCCAAAGACCACTGTGAT
CCTAAGGTGCTCTGCATAATCAACCCTGGGAACCCCACAGGCCAGGTACAAAGCAGAAAG
TGCATAGAAGATGTGATCCACTTTGCCTGGGAAGAGAAGCTCTTTCTCCTGGCTGATGAG
GTGTACCAGGACAACGTGTACTCTCCAGATTGCAGATTCCACTCCTTCAAGAAGGTGCTG
TACGAGATGGGGCCCGAGTACTCCAGCAACGTGGAGCTCGCCTCCTTCCACTCCACCTCC
AAGGGCTACATGGGCGAGTGTGGTTACAGAGGAGGCTACATGGAGGTGATCAACCTGCAC
CCTGAGATCAAGGGCCAGCTGGTGAAGCTGCTGTCGGTGCGCCTGTGCCCCCCAGTGTCT
GGGCAGGCCGCCATGGACATTGTCGTGAACCCCCCGGTGGCAGGAGAGGAGTCCTTTGAG
CAATTCAGCCGAGAGAAGGAGTCGGTCCTGGGTAATCTGGCCAAAAAAGCAAAGCTGACG
GAAGACCTGTTTAACCAAGTCCCAGGAATTCACTGCAACCCCTTGCAGGGGGCCATGTAC
GCCTTCCCTCGGATCTTCATTCCTGCCAAAGCTGTGGAGGCTGCTCAGGCCCATCAAATG
GCTCCAGACATGTTCTACTGCATGAAGCTCCTGGAGGAGACTGGCATCTGTGTCGTGCCC
GGCAGTGGCTTTGGGCAGAGGGAAGGCACTTACCACTTCAGGATGACTATCCTCCCTCCA
GTGGAGAAGCTGAAAACGGTGCTGCAGAAGGTGAAAGACTTCCACATCAACTTCCTGGAG
AAGTACGCGTGA
|
| Enzyme 11 GenBank Gene ID |
AY029173  |
| Enzyme 11 GeneCard ID |
GPT2  |
| Enzyme 11 GenAtlas ID |
GPT2  |
| Enzyme 11 HGNC ID |
HGNC:18062  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
16q12.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
10418 |
| Enzyme 12 Name |
Selenocysteine lyase |
| Enzyme 12 Synonyms |
- hSCL
|
| Enzyme 12 Gene Name |
SCLY |
| Enzyme 12 Protein Sequence |
>Selenocysteine lyase
MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGN
PSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTS
KGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQAEVDDI
LAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGK
QRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTP
MIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCN
FSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGR
STTRAEVDLVVQDLKQAVAQLEDQA
|
| Enzyme 12 Number of Residues |
445 |
| Enzyme 12 Molecular Weight |
48148.4 |
| Enzyme 12 Theoretical pI |
7.13 |
| Enzyme 12 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in metabolic process |
| Enzyme 12 Specific Function |
Catalyzes the decomposition of L-selenocysteine to L- alanine and elemental selenium |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
- L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor [RN:R03598]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
156713448  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q96I15  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
SCLY_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1338 bp
ATGGAGGCGGCCGTGGCGCCGGGGAGGGATGCGCCGGCACCCGCGGCGAGTCAGCCCAGC
GGCTGCGGGAAACACAACTCGCCGGAGAGGAAAGTTTATATGGACTATAATGCAACGACT
CCCCTGGAGCCAGAAGTTATCCAGGCCATGACCAAGGCCATGTGGGAAGCCTGGGGAAAT
CCCAGCAGCCCGTATTCAGCAGGAAGAAAGGCCAAGGATATTATAAATGCAGCTCGGGAA
AGCCTCGCGAAGATGATAGGGGGGAAACCTCAAGATATAATCTTCACTTCCGGGGGCACT
GAGTCAAATAATTTAGTAATCCATTCTGTGGTGAAACATTTCCACGCAAACCAGACCTCA
AAGGGACACACAGGTGGGCACCACAGCCCAGTGAAGGGGGCCAAGCCCCATTTCATTACT
TCCTCGGTGGAACACGACTCCATCCGGCTGCCCCTGGAGCACCTGGTGGAAGAACAAGTG
GCAGCGGTCACCTTTGTCCCGGTGTCCAAGGTGAGCGGGCAGGCAGAGGTGGACGACATC
CTCGCGGCAGTCCGCCCGACCACACGCCTCGTGACCATCATGCTGGCCAACAATGAGACT
GGCATTGTCATGCCTGTCCCTGAAATCAGTCAGCGCATTAAAGCCCTGAACCAGGAACGG
GTGGCAGCTGGGCTACCTCCCATCCTCGTGCACACGGATGCTGCACAGGCCTTGGGGAAG
CAGCGCGTGGATGTGGAGGACCTGGGCGTGGACTTCCTTACAATCGTGGGGCACAAGTTT
TATGGTCCCAGGATTGGCGCACTTTATATACGAGGACTTGGTGAATTTACCCCTCTCTAC
CCTATGCTATTTGGAGGTGGACAAGAACGGAATTTCAGGCCAGGGACAGAGAACACCCCA
ATGATTGCTGGCCTTGGGAAGGCCGCGGAGCTGGTGACCCAGAACTGCGAGGCTTATGAG
GCCCACATGAGGGACGTCCGCGACTACCTGGAAGAGAGGCTGGAAGCTGAATTCGGTCAG
AAGAGAATCCATCTGAATAGCCAGTTTCCAGGCACCCAGCGGCTTCCCAATACCTGTAAC
TTTTCCATCCGGGGACCCCGGCTTCAAGGCCACGTGGTGCTTGCGCAGTGCCGAGTGCTG
ATGGCCAGTGTGGGGGCCGCGTGCCACTCGGACCACGGGGACCAGCCGTCCCCAGTGCTG
CTGAGCTACGGTGTCCCCTTCGACGTGGCCAGGAACGCGCTCCGGCTCAGCGTGGGCCGC
AGCACCACCAGGGCCGAGGTGGACCTCGTCGTGCAGGACCTGAAGCAGGCCGTGGCGCAG
CTGGAGGACCAGGCCTAG
|
| Enzyme 12 GenBank Gene ID |
NM_016510.4  |
| Enzyme 12 GeneCard ID |
SCLY  |
| Enzyme 12 GenAtlas ID |
SCLY  |
| Enzyme 12 HGNC ID |
HGNC:18161  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
2q37.3 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Mihara H, Kurihara T, Watanabe T, Yoshimura T, Esaki N: cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis. J Biol Chem. 2000 Mar 3;275(9):6195-200. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Jafari C, Panzer U, Steinmetz OM, Zahner G, Stahl RA, Harendza S: Enhanced expression of selenocysteine lyase in acute glomerulonephritis and its regulation by AP-1. Cell Mol Biol Lett. 2006;11(3):424-37. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
12977 |
| Enzyme 13 Name |
Alanine aminotransferase |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
GPT |
| Enzyme 13 Protein Sequence |
>Alanine aminotransferase
MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPF
TEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSL
GAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRT
GVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVI
NPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPY
AGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDL
VVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQL
PPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLL
LEKLSRFHAKFTLEYS
|
| Enzyme 13 Number of Residues |
496 |
| Enzyme 13 Molecular Weight |
54637 |
| Enzyme 13 Theoretical pI |
Not Available |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
Not Available |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
Not Available |
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
Not Available |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
B0YJ18  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
B0YJ18_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
Not Available |
| Enzyme 13 GenBank Gene ID |
Not Available |
| Enzyme 13 GeneCard ID |
B0YJ18  |
| Enzyme 13 GenAtlas ID |
Not Available |
| Enzyme 13 HGNC ID |
Not Available |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
Not Available |
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
13118 |
| Enzyme 14 Name |
Kynureninase (L-kynurenine hydrolase) |
| Enzyme 14 Synonyms |
- SubName: Kynureninase (L-kynurenine hydrolase), isoform CRA_a
|
| Enzyme 14 Gene Name |
KYNU |
| Enzyme 14 Protein Sequence |
>Kynureninase (L-kynurenine hydrolase)
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
|
| Enzyme 14 Number of Residues |
307 |
| Enzyme 14 Molecular Weight |
34634.5 |
| Enzyme 14 Theoretical pI |
5.71 |
| Enzyme 14 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on acid carbon-carbon bonds
- hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
- kynureninase activity
- pyridoxal phosphate binding
|
| Process |
- NAD biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- indolalkylamine metabolic process
- metabolic process
- nicotinamide nucleotide biosynthetic process
- pyridine nucleotide biosynthetic process
- tryptophan catabolic process
- tryptophan metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 14 General Function |
Involved in metabolic process |
| Enzyme 14 Specific Function |
Not Available |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
12654129  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9BVW3  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
Q9BVW3_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>924 bp
ATGGAGCCTTCATCTCTTGAGCTGCCGGCTGACACAGTGCAGCGCATTGCGGCTGAACTC
AAATGCCACCCAACGGATGAGAGGGTGGCTCTCCACCTAGATGAGGAAGATAAGCTGAGG
CACTTCAGGGAGTGCTTTTATATTCCCAAAATACAGGATCTGCCTCCAGTTGATTTATCA
TTAGTGAATAAAGATGAAAATGCCATCTATTTCTTGGGAAATTCTCTTGGCCTTCAACCA
AAAATGGTTAAAACATATCTTGAAGAAGAACTAGATAAGTGGGCCAAAATAGCAGCCTAT
GGTCATGAAGTGGGGAAGCGTCCTTGGATTACAGGAGATGAGAGTATTGTAGGCCTTATG
AAGGACATTGTAGGAGCCAATGAGAAAGAAATAGCCCTAATGAATGCTTTGACTGTAAAT
TTACATCTTCTAATGTTATCATTTTTTAAGCCTACGCCAAAACGATATAAAATTCTTCTA
GAAGCCAAAGCCTTCCCTTCTGATCATTATGCTATTGAGTCACAACTACAACTTCACGGA
CTTAACATTGAAGAAAGTATGCGGATGATAAAGCCAAGAGAGGGGGAAGAAACCTTAAGA
ATAGAGGATATCCTTGAAGTAATTGAGAAGGAAGGAGACTCAATTGCAGTGATCCTGTTC
AGTGGGGTGCATTTTTACACTGGACAGCACTTTAATATTCCTGCCATCACAAAAGCTGGA
CAAGCGAAGGGTTGTTATGTTGGCTTTGATCTAGCACATGCAGTTGGAAATGTTGAACTC
TACTTACATGACTGGGGAGTTGATTTTGCCTGCTGGTGTTCCTACAAGTATTTAAATGCA
GGAGCAGGAGGAATTGCTGGTGCCTTCATTCATGAAAAGCATGCCCATACGATTAAACCT
GCGAGATCGGAGTTCTTTAATTAG
|
| Enzyme 14 GenBank Gene ID |
BC000879  |
| Enzyme 14 GeneCard ID |
KYNU  |
| Enzyme 14 GenAtlas ID |
KYNU  |
| Enzyme 14 HGNC ID |
HGNC:6469  |
| Enzyme 14 Chromosome Location |
2 |
| Enzyme 14 Locus |
2q22.2 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
14700 |
| Enzyme 15 Name |
Alanine--glyoxylate aminotransferase 2-like 2 |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
AGXT2L2 |
| Enzyme 15 Protein Sequence |
>Alanine--glyoxylate aminotransferase 2-like 2
MAADQRPKADTLALRQRLISSSCRLFFPEDPVKIVRAQGQYMYDEQGAEYIDCISNVAHV
GHCHPLVVQAAHEQNQVLNTNSRYLHDNIVDYAQRLSETLPEQLCVFYFLNSGSEANDLA
LRLARHYTGHQDVVVLDHAYHGHLSSLIDISPYKFRNLDGQKEWVHVAPLPDTYRGPYRE
DHPNPAMAYANEVKRVVSSAQEKGRKIAAFFAESLPSVGGQIIPPAGYFSQVAEHIRKAG
GVFVADEIQVGFGRVGKHFWAFQLQGKDFVPDIVTMGKSIGNGHPVACVAATQPVARAFE
ATGVEYFNTFGGSPVSCAVGLAVLNVLEKEQLQDHATSVGSFLMQLLGQQKIKHPIVGDV
RGVGLFIGVDLIKDEATRTPATEEAAYLVSRLKENYVLLSTDGPGRNILKFKPPMCFSLD
NARQVVAKLDAILTDMEEKVRSCETLRLQP
|
| Enzyme 15 Number of Residues |
450 |
| Enzyme 15 Molecular Weight |
49710.2 |
| Enzyme 15 Theoretical pI |
6.76 |
| Enzyme 15 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in transaminase activity |
| Enzyme 15 Specific Function |
Not Available |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
24119277  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q8IUZ5  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
AT2L2_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1353 bp
ATGGCCGCAGACCAGCGCCCGAAGGCCGACACGCTGGCCCTGAGGCAACGGCTCATCAGC
TCTTCCTGCAGACTCTTTTTTCCCGAGGATCCTGTTAAGATTGTCCGGGCCCAAGGGCAG
TACATGTACGATGAACAGGGGGCAGAATACATCGATTGCATCAGCAATGTGGCGCACGTT
GGGCACTGCCACCCTCTCGTGGTCCAAGCAGCACATGAGCAGAACCAGGTGCTCAACACC
AACAGCCGGTACCTGCATGACAACATCGTGGACTATGCGCAGAGGCTGTCAGAGACCCTG
CCGGAGCAGCTCTGTGTGTTCTATTTCCTGAATTCTGGGTCAGAAGCCAATGACCTGGCC
CTGAGGCTGGCTCGCCACTACACGGGACACCAGGACGTGGTGGTATTAGATCATGCGTAT
CACGGCCACCTGAGCTCCCTGATTGACATCAGTCCCTACAAGTTCCGCAACCTGGATGGC
CAGAAGGAGTGGGTCCACGTGGCACCTCTCCCAGACACCTACCGGGGCCCCTACCGGGAG
GACCACCCCAACCCAGCTATGGCCTATGCCAACGAGGTGAAACGTGTGGTCAGCAGTGCA
CAGGAGAAGGGCAGGAAGATTGCAGCCTTCTTCGCTGAGTCTCTGCCCAGTGTGGGAGGG
CAGATCATTCCCCCTGCTGGCTACTTCTCCCAAGTGGCAGAGCACATCCGCAAGGCCGGA
GGGGTCTTTGTTGCAGATGAGATCCAGGTTGGCTTTGGCCGGGTAGGCAAGCACTTCTGG
GCCTTCCAGCTCCAGGGAAAAGACTTCGTCCCTGACATCGTCACCATGGGCAAGTCCATT
GGCAACGGCCACCCTGTTGCCTGCGTGGCCGCAACCCAGCCTGTGGCGAGGGCATTTGAA
GCCACCGGCGTTGAGTACTTCAACACGTTTGGGGGCAGCCCAGTGTCCTGCGCTGTGGGG
CTGGCCGTCCTGAATGTCTTGGAGAAGGAGCAGCTCCAGGATCATGCCACCAGTGTAGGC
AGCTTCCTGATGCAGCTCCTCGGGCAGCAAAAAATCAAACATCCCATCGTCGGGGATGTC
AGGGGTGTTGGGCTCTTCATTGGTGTGGATCTGATCAAAGATGAGGCCACAAGGACACCA
GCAACTGAAGAGGCTGCCTACTTGGTATCAAGGCTGAAGGAGAACTACGTTTTGCTGAGC
ACTGATGGCCCTGGGAGGAACATCCTGAAGTTTAAGCCCCCAATGTGCTTCAGCCTGGAC
AATGCACGGCAGGTGGTGGCAAAGCTGGATGCCATTCTGACTGACATGGAAGAGAAGGTG
AGAAGTTGTGAAACGCTGAGGCTCCAGCCCTAA
|
| Enzyme 15 GenBank Gene ID |
NM_153373.2  |
| Enzyme 15 GeneCard ID |
AGXT2L2  |
| Enzyme 15 GenAtlas ID |
AGXT2L2  |
| Enzyme 15 HGNC ID |
HGNC:28249  |
| Enzyme 15 Chromosome Location |
5 |
| Enzyme 15 Locus |
5q35.3 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J: Large-scale cDNA transfection screening for genes related to cancer development and progression. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15724-9. Epub 2004 Oct 21. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
15229 |
| Enzyme 16 Name |
cDNA FLJ77866, highly similar to Homo sapiens peptidoglycan recognition protein L (PGLYRP) mRNA (Peptidoglycan recognition protein 2, isoform CRA_a) |
| Enzyme 16 Synonyms |
Not Available |
| Enzyme 16 Gene Name |
PGLYRP2 |
| Enzyme 16 Protein Sequence |
>cDNA FLJ77866, highly similar to Homo sapiens peptidoglycan recognition protein L (PGLYRP) mRNA (Peptidoglycan recognition protein 2, isoform CRA_a)
MAQGVLWILLGLLLWSDPGTASLPLLMDSVIQALAELEQKVPAAKTRHTASAWLMSAPNS
GPHNRLYHFLLGAWSLNATELDPCPLSPELLGLTKEVARHDVREGKEYGVVLAPDGSTVA
VEPLLAGLEAGLQGRRVINLPLDSMAAPWETGDTFPDVVAIAPDVRATSSPGLRDGSPDV
TTADIGANTPDATKGCPDVQASLPDAKAKSPPTMVDSLLAVTLAGNLGLTFLRGSQTQSH
PDLGTEGCWDQLSAPRTFTLLDPKASLLTMAFLNGALDGVILGDYLSRTPEPRPSLSHLL
SQYYGAGVARDPGFRSNFRRQNGAALTSASILAQQVWGTLVLLQRLEPVHLQLQCMSQEQ
LAQVAANATKEFTEAFLGCPAIHPRCRWGAAPYRGRPKLLQLPLGFLYVHHTYVPAPPCT
DFTRCAANMRSMQRYHQDTQGWGDIGYSFVVGSDGYVYEGRGWHWVGAHTLGHNSRGFGV
AIVGNYTAALPTEAALRTVRDTLPSCAVRAGLLRPDYALLGHRQLVRTDCPGDALFDLLR
TWPHFTATVKPRPARSVSKRSRREPPPRTLPATDLQ
|
| Enzyme 16 Number of Residues |
576 |
| Enzyme 16 Molecular Weight |
62218 |
| Enzyme 16 Theoretical pI |
7.59 |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Not Available |
| Enzyme 16 Specific Function |
Not Available |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
Not Available |
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
158258016  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
A8K8C7  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
A8K8C7_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1731 bp
ATGGCCCAGGGTGTCCTCTGGATCCTACTCGGATTGCTACTGTGGTCAGACCCAGGGACA
GCCTCCCTGCCCCTGCTCATGGACTCTGTCATCCAGGCCCTGGCTGAGCTGGAGCAGAAA
GTGCCAGCTGCCAAGACCAGACACACAGCTTCTGCGTGGCTGATGTCAGCTCCAAACTCT
GGCCCCCACAATCGCCTCTACCACTTCCTGCTGGGGGCATGGAGCCTCAATGCTACAGAG
TTGGATCCCTGCCCACTAAGCCCAGAGCTGTTAGGCCTGACCAAGGAGGTGGCCCGACAT
GACGTACGAGAAGGGAAGGAATATGGGGTGGTGCTGGCACCTGATGGCTCGACCGTGGCT
GTGGAGCCTCTGCTGGCGGGGCTGGAGGCAGGGCTGCAAGGGCGCAGGGTCATAAATTTG
CCCTTGGACAGCATGGCTGCCCCTTGGGAGACTGGAGATACCTTTCCAGATGTTGTGGCC
ATTGCTCCAGATGTAAGAGCCACCTCCTCCCCAGGACTCAGGGATGGCTCTCCAGATGTC
ACCACTGCAGATATTGGAGCCAACACTCCAGATGCTACAAAAGGCTGTCCAGATGTCCAA
GCTTCCTTGCCAGATGCCAAAGCCAAGTCCCCACCGACCATGGTGGACAGCCTCCTGGCA
GTCACCCTGGCTGGAAACCTGGGCCTGACCTTCCTCCGAGGTTCCCAGACCCAGAGCCAT
CCAGACCTGGGAACTGAGGGCTGCTGGGACCAGCTCTCTGCCCCTCGGACCTTTACGCTT
TTGGACCCCAAGGCATCTCTGTTAACCATGGCCTTCCTCAATGGCGCCCTGGATGGGGTC
ATCCTTGGAGACTACCTGAGCCGGACTCCTGAGCCCCGGCCATCCCTCAGCCACTTGCTG
AGCCAGTACTATGGGGCTGGGGTGGCCAGAGACCCAGGGTTCCGCAGCAACTTCCGACGG
CAGAACGGTGCTGCTCTGACTTCAGCCTCCATCCTGGCCCAGCAGGTGTGGGGAACCCTT
GTCCTTCTACAGAGGCTGGAGCCAGTACACCTCCAGCTTCAGTGCATGAGCCAAGAACAG
CTGGCCCAGGTGGCTGCCAATGCTACCAAGGAATTCACTGAGGCCTTCCTGGGATGCCCG
GCCATCCACCCCCGCTGCCGCTGGGGAGCGGCGCCTTATCGGGGCCGCCCGAAGCTGCTG
CAGCTGCCGCTGGGATTCTTGTACGTGCATCACACCTACGTGCCTGCACCACCCTGCACG
GACTTCACGCGCTGCGCAGCCAACATGCGCTCCATGCAGCGCTACCACCAGGACACGCAA
GGCTGGGGAGACATCGGCTACAGTTTCGTGGTGGGCTCGGACGGCTACGTGTACGAGGGA
CGCGGCTGGCACTGGGTGGGCGCCCACACGCTCGGCCACAACTCCCGGGGCTTCGGCGTG
GCCATAGTGGGCAACTACACCGCGGCGCTGCCCACCGAGGCCGCTCTGCGCACGGTGCGC
GACACGCTCCCGAGTTGTGCGGTGCGCGCCGGCCTCCTGCGGCCAGACTACGCGCTGCTG
GGCCACCGCCAGCTGGTGCGCACCGACTGCCCCGGCGACGCGCTCTTCGACCTGCTGCGC
ACCTGGCCGCACTTCACCGCGACTGTTAAGCCAAGACCTGCCAGGAGTGTCTCTAAGAGA
TCCAGGAGGGAGCCACCCCCAAGGACCCTGCCAGCCACAGACCTCCAATAA
|
| Enzyme 16 GenBank Gene ID |
AK292292  |
| Enzyme 16 GeneCard ID |
A8K8C7  |
| Enzyme 16 GenAtlas ID |
Not Available |
| Enzyme 16 HGNC ID |
Not Available |
| Enzyme 16 Chromosome Location |
19 |
| Enzyme 16 Locus |
19p13.12 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
Not Available |
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
15230 |
| Enzyme 17 Name |
Peptidoglycan recognition protein 3 |
| Enzyme 17 Synonyms |
- Peptidoglycan recognition protein I-alpha
- PGLYRPIalpha
- PGRP-I-alpha
- Peptidoglycan recognition protein intermediate alpha
|
| Enzyme 17 Gene Name |
PGLYRP3 |
| Enzyme 17 Protein Sequence |
>Peptidoglycan recognition protein 3
MGTLPWLLAFFILGLQAWDTPTIVSRKEWGARPLACRALLTLPVAYIITDQLPGMQCQQQ
SVCSQMLRGLQSHSVYTIGWCDVAYNFLVGDDGRVYEGVGWNIQGLHTQGYNNISLGIAF
FGNKIGSSPSPAALSAAEGLISYAIQKGHLSPRYIQPLLLKEETCLDPQHPVMPRKVCPN
IIKRSAWEARETHCPKMNLPAKYVIIIHTAGTSCTVSTDCQTVVRNIQSFHMDTRNFCDI
GYHFLVGQDGGVYEGVGWHIQGSHTYGFNDIALGIAFIGYFVEKPPNAAALEAAQDLIQC
AVVEGYLTPNYLLMGHSDVVNILSPGQALYNIISTWPHFKH
|
| Enzyme 17 Number of Residues |
341 |
| Enzyme 17 Molecular Weight |
37611.0 |
| Enzyme 17 Theoretical pI |
6.96 |
| Enzyme 17 GO Classification |
| Function |
- N-acetylmuramoyl-L-alanine amidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
- protein binding
|
| Process |
- aminoglycan metabolic process
- carbohydrate metabolic process
- glycosaminoglycan metabolic process
- metabolic process
- peptidoglycan catabolic process
- peptidoglycan metabolic process
- polysaccharide metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in N-acetylmuramoyl-L-alanine amidase activity |
| Enzyme 17 Specific Function |
Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
Not Available |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q96LB9  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
PGRP3_HUMAN  |
| Enzyme 17 PDB ID |
1SK3  |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1026 bp
ATGGGGACGCTGCCATGGCTTCTTGCCTTCTTCATTCTGGGTCTCCAGGCTTGGGATACT
CCCACCATCGTCTCCCGCAAGGAGTGGGGGGCAAGACCGCTCGCCTGCAGGGCCCTGCTG
ACCCTGCCTGTGGCCTACATCATCACAGACCAGCTCCCAGGGATGCAGTGCCAGCAGCAG
AGCGTTTGCAGCCAGATGCTGCGGGGGTTGCAGTCCCATTCCGTCTACACCATAGGCTGG
TGCGACGTGGCGTACAACTTCCTGGTTGGGGATGATGGCAGGGTGTATGAAGGTGTTGGC
TGGAACATCCAAGGCTTGCACACCCAGGGCTACAACAACATTTCCCTGGGCATCGCCTTC
TTTGGCAATAAGATAGGCAGCAGTCCCAGCCCTGCTGCCTTATCAGCTGCAGAGGGTCTG
ATCTCCTATGCCATCCAGAAGGGTCACCTGTCGCCCAGGTATATTCAGCCACTTCTTCTG
AAAGAAGAGACCTGCCTGGACCCTCAACATCCAGTGATGCCCAGGAAGGTTTGCCCCAAC
ATCATCAAACGATCTGCTTGGGAAGCCAGAGAGACACACTGCCCTAAAATGAACCTCCCA
GCCAAATATGTCATCATCATCCACACCGCTGGCACAAGCTGCACTGTATCCACAGACTGC
CAGACTGTCGTCCGAAACATACAGTCCTTTCACATGGACACACGGAACTTTTGTGACATT
GGATATCACTTCCTGGTGGGCCAGGATGGTGGCGTGTATGAAGGGGTTGGATGGCACATC
CAAGGCTCTCACACTTATGGATTCAACGATATTGCCCTAGGAATTGCCTTCATCGGCTAC
TTTGTAGAAAAGCCTCCAAATGCTGCAGCGCTGGAGGCGGCCCAGGACCTGATCCAGTGT
GCCGTGGTTGAGGGGTACCTGACTCCAAACTACCTGCTGATGGGCCACAGTGACGTGGTC
AACATCCTGTCCCCTGGGCAGGCTTTGTATAACATCATCAGCACCTGGCCTCATTTCAAG
CACTGA
|
| Enzyme 17 GenBank Gene ID |
AY035376  |
| Enzyme 17 GeneCard ID |
PGLYRP3  |
| Enzyme 17 GenAtlas ID |
PGLYRP3  |
| Enzyme 17 HGNC ID |
HGNC:30014  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
1q21 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Liu C, Xu Z, Gupta D, Dziarski R: Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules. J Biol Chem. 2001 Sep 14;276(37):34686-94. Epub 2001 Jul 18. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lu X, Wang M, Qi J, Wang H, Li X, Gupta D, Dziarski R: Peptidoglycan recognition proteins are a new class of human bactericidal proteins. J Biol Chem. 2006 Mar 3;281(9):5895-907. Epub 2005 Dec 14. [PubMed
]
- Guan R, Malchiodi EL, Wang Q, Schuck P, Mariuzza RA: Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha. J Biol Chem. 2004 Jul 23;279(30):31873-82. Epub 2004 May 12. [PubMed
]
- Guan R, Roychowdhury A, Ember B, Kumar S, Boons GJ, Mariuzza RA: Structural basis for peptidoglycan binding by peptidoglycan recognition proteins. Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17168-73. Epub 2004 Nov 30. [PubMed
]
- Guan R, Brown PH, Swaminathan CP, Roychowdhury A, Boons GJ, Mariuzza RA: Crystal structure of human peptidoglycan recognition protein I alpha bound to a muramyl pentapeptide from Gram-positive bacteria. Protein Sci. 2006 May;15(5):1199-206. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
15231 |
| Enzyme 18 Name |
Peptidoglycan recognition protein 4 (PGLYRP4 protein) |
| Enzyme 18 Synonyms |
Not Available |
| Enzyme 18 Gene Name |
PGLYRP4 |
| Enzyme 18 Protein Sequence |
>Peptidoglycan recognition protein 4 (PGLYRP4 protein)
MLPWLLVFSALGIQAWGDSSWNKTQAKQVSEGLQYLFENISQLTEKGLPTDVSTTVSRKA
WGAEAVGCSIQLTTPVNVLVIHHVPGLECHDQTVCSQRLRELQAHHVHNNSGCDVAYNFL
VGDDGRVYEGVGWNIQGVHTQGYNNISLGFAFFGTKKGHSPSPAALSAMENLITYAVQKG
HLSSSYVQPLLGKGENCLAPRQKTSLKKACPGVVPRSVWGARETHCPRMTLPAKYGIIIH
TAGRTCNISDECRLLVRDIQSFYIDRLKSCDIGYNFLVGQDGAIYEGVGWNVQGSSTPGY
DDIALGITFMGTFTGIPPNAAALEAAQDLIQCAMVKGYLTPNYLLVGHSDVARTLSPGQA
LYNIISTWPHFKH
|
| Enzyme 18 Number of Residues |
373 |
| Enzyme 18 Molecular Weight |
40621 |
| Enzyme 18 Theoretical pI |
7.53 |
| Enzyme 18 GO Classification |
| Function |
- N-acetylmuramoyl-L-alanine amidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
- protein binding
|
| Process |
- carbohydrate metabolism
- cellular carbohydrate metabolism
- macromolecule metabolism
- metabolism
- peptidoglycan catabolism
- peptidoglycan metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Not Available |
| Enzyme 18 Specific Function |
Not Available |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
148744335  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q5SY64  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
Q5SY64_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1122 bp
ATGCTGCCGTGGCTTCTTGTCTTCTCTGCTCTGGGTATCCAGGCCTGGGGTGATTCCTCC
TGGAACAAAACACAAGCTAAACAGGTATCAGAGGGGCTCCAGTACCTATTTGAGAACATC
TCCCAGCTCACTGAAAAAGGCCTTCCCACAGATGTCTCCACCACGGTCTCTCGCAAGGCA
TGGGGGGCAGAAGCTGTTGGCTGCAGTATTCAGCTGACCACGCCAGTGAATGTCCTTGTT
ATACACCATGTCCCTGGACTGGAGTGTCACGACCAGACAGTCTGCAGCCAGAGACTGCGG
GAACTGCAGGCCCATCATGTCCACAACAACAGTGGGTGTGATGTGGCCTACAACTTCCTG
GTTGGGGATGATGGCAGGGTGTATGAAGGTGTTGGCTGGAATATCCAAGGAGTGCACACC
CAAGGCTACAACAACATCTCCCTGGGCTTTGCCTTCTTTGGCACTAAGAAAGGCCACAGT
CCCAGCCCTGCTGCCCTGTCGGCCATGGAAAACCTAATCACCTATGCTGTCCAGAAGGGC
CACCTGTCATCCAGTTATGTTCAGCCACTTCTTGGGAAAGGCGAGAACTGCCTGGCCCCT
CGGCAGAAGACAAGCCTGAAGAAGGCTTGCCCCGGCGTTGTCCCACGGTCTGTGTGGGGA
GCCAGGGAGACCCACTGTCCCAGGATGACTCTCCCAGCGAAGTATGGCATCATTATCCAC
ACTGCCGGGAGGACCTGCAACATTTCTGATGAGTGCCGCCTGCTGGTCCGGGACATCCAG
TCTTTCTACATAGACAGGCTCAAGTCATGCGACATTGGTTATAACTTCCTGGTGGGCCAG
GATGGCGCCATTTATGAAGGGGTGGGCTGGAATGTCCAAGGCTCCTCCACCCCTGGCTAC
GATGACATTGCCCTGGGCATTACCTTCATGGGCACCTTCACAGGTATACCACCCAATGCT
GCAGCACTAGAGGCAGCCCAAGACCTGATCCAGTGTGCCATGGTCAAAGGGTACCTGACT
CCCAACTACCTGCTGGTGGGCCACAGTGATGTGGCCCGAACCTTGTCTCCTGGGCAGGCT
TTGTACAACATCATCAGCACCTGGCCTCATTTCAAACACTGA
|
| Enzyme 18 GenBank Gene ID |
BC142636  |
| Enzyme 18 GeneCard ID |
Q5SY64  |
| Enzyme 18 GenAtlas ID |
PGLYRP4  |
| Enzyme 18 HGNC ID |
HGNC:30015  |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
16505 |
| Enzyme 19 Name |
cDNA FLJ10608 fis, clone NT2RP2005239, highly similar to Cysteine desulfurase, mitochondrial (EC 2.8.1.7) |
| Enzyme 19 Synonyms |
- SubName: NFS1 nitrogen fixation 1 (S. cerevisiae), isoform CRA_a
|
| Enzyme 19 Gene Name |
NFS1 |
| Enzyme 19 Protein Sequence |
>cDNA FLJ10608 fis, clone NT2RP2005239, highly similar to Cysteine desulfurase, mitochondrial (EC 2.8.1.7)
MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLY
MDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPRE
IIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQK
SGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKI
PLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPL
VVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAY
VEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD
YTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH
|
| Enzyme 19 Number of Residues |
457 |
| Enzyme 19 Molecular Weight |
50196 |
| Enzyme 19 Theoretical pI |
8.45 |
| Enzyme 19 GO Classification |
| Function |
- binding
- catalytic activity
- cysteine desulfurase activity
- pyridoxal phosphate binding
- sulfurtransferase activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
- transferase activity, transferring sulfur-containing groups
- vitamin binding
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- cysteine metabolism
- metabolism
- physiological process
- sulfur amino acid metabolism
|
| Component |
| — |
|
| Enzyme 19 General Function |
Amino acid transport and metabolism |
| Enzyme 19 Specific Function |
Not Available |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
- L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine ALL_REAC (other) R07460
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
Not Available |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
B3KMA5  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
B3KMA5_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
Not Available |
| Enzyme 19 GenBank Gene ID |
AK001470  |
| Enzyme 19 GeneCard ID |
B3KMA5  |
| Enzyme 19 GenAtlas ID |
Not Available |
| Enzyme 19 HGNC ID |
Not Available |
| Enzyme 19 Chromosome Location |
20 |
| Enzyme 19 Locus |
20q11.22 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
Not Available |
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
16929 |
| Enzyme 20 Name |
Probable alanyl-tRNA synthetase, mitochondrial |
| Enzyme 20 Synonyms |
- Alanine--tRNA ligase
- AlaRS
- Alanyl-tRNA synthetase-like
|
| Enzyme 20 Gene Name |
AARS2 |
| Enzyme 20 Protein Sequence |
>Probable alanyl-tRNA synthetase, mitochondrial
MAASVAAAARRLRRAIRRSPAWRGLSHRPLSSEPPAAKASAVRAAFLNFFRDRHGHRLVP
SASVRPRGDPSLLFVNAGMNQFKPIFLGTVDPRSEMAGFRRVANSQKCVRAGGHHNDLED
VGRDLSHHTFFEMLGNWAFGGEYFKEEACNMAWELLTQVYGIPEERLWISYFDGDPKAGL
DPDLETRDIWLSLGVPASRVLSFGPQENFWEMGDTGPCGPCTEIHYDLAGGVGAPQLVEL
WNLVFMQHNREADGSLQPLPQRHVDTGMGLERLVAVLQGKHSTYDTDLFSPLLNAIQQGC
RAPPYLGRVGVADEGRTDTAYRVVADHIRTLSVCISDGIFPGMSGPPLVLRRILRRAVRF
SMEILKAPPGFLGSLVPVVVETLGDAYPELQRNSAQIANLVSEDEAAFLASLERGRRIID
RTLRTLGPSDMFPAEVAWSLSLCGDLGLPLDMVELMLEEKGVQLDSAGLERLAQEEAQHR
ARQAEPVQKQGLWLDVHALGELQRQGVPPTDDSPKYNYSLRPSGSYEFGTCEAQVLQLYT
EDGTAVASVGKGQRCGLLLDRTNFYAEQGGQASDRGYLVRAGQEDVLFPVARAQVCGGFI
LHEAVAPECLRLGDQVQLHVDEAWRLGCMAKHTATHLLNWALRQTLGPGTEQQGSHLNPE
QLRLDVTTQTPLTPEQLRAVENTVQEAVGQDEAVYMEEVPLALTAQVPGLRSLDEVYPDP
VRVVSVGVPVAHALDPASQAALQTSVELCCGTHLLRTGAVGDLVIIGDRQLSKGTTRLLA
VTGEQAQQARELGQSLAQEVKAATERLSLGSRDVAEALRLSKDIGRLIEAVETAVMPQWQ
RRELLATVKMLQRRANTAIRKLQMGQAAKKTQELLERHSKGPLIVDTVSAESLSVLVKVV
RQLCEQAPSTSVLLLSPQPMGKVLCACQVAQGAMPTFTAEAWALAVCSHMGGKAWGSRVV
AQGTGSTTDLEAALSIAQTYALSQL
|
| Enzyme 20 Number of Residues |
985 |
| Enzyme 20 Molecular Weight |
107339.5 |
| Enzyme 20 Theoretical pI |
6.20 |
| Enzyme 20 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- alanine-tRNA ligase activity
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- alanyl-tRNA aminoacylation
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 20 General Function |
Involved in nucleotide binding |
| Enzyme 20 Specific Function |
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction:alanine is first activated by ATP to form Ala- AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
- ATP + L-alanine + tRNAAla = AMP + diphosphate + L-alanyl-tRNAAla [RN:R03038]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
38569417  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q5JTZ9  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
SYAM_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>2958 bp
ATGGCAGCGTCAGTGGCAGCTGCAGCCCGGAGGCTGCGGCGGGCCATTCGAAGGTCGCCC
GCATGGCGGGGCCTCAGCCATCGGCCGCTCTCATCGGAGCCCCCTGCAGCCAAGGCCTCG
GCCGTGAGGGCCGCCTTTCTGAACTTCTTTCGGGACCGCCATGGCCACCGGCTGGTGCCC
TCCGCTTCCGTGCGGCCCCGCGGCGACCCCAGTTTGCTTTTTGTCAATGCGGGCATGAAC
CAGTTCAAGCCAATCTTTCTGGGCACCGTGGATCCACGAAGCGAGATGGCAGGCTTCCGA
CGTGTGGCCAACAGCCAGAAATGTGTGAGAGCTGGAGGACACCATAACGACCTGGAAGAT
GTGGGTCGAGACCTTTCCCATCATACCTTCTTTGAAATGCTTGGCAATTGGGCCTTTGGG
GGTGAATATTTTAAGGAGGAGGCTTGTAACATGGCCTGGGAACTGCTGACTCAGGTCTAT
GGGATCCCTGAGGAAAGGCTCTGGATCTCCTACTTTGATGGTGACCCCAAGGCAGGGCTG
GACCCAGACCTGGAGACCAGGGACATCTGGCTGAGCTTAGGGGTGCCTGCTAGCCGTGTG
CTTTCCTTTGGACCACAAGAGAACTTCTGGGAGATGGGGGATACTGGCCCTTGTGGGCCC
TGTACTGAGATCCACTACGACCTTGCTGGTGGGGTGGGAGCCCCCCAGCTGGTAGAGCTT
TGGAACCTGGTCTTCATGCAACACAACAGAGAGGCAGATGGAAGCCTGCAGCCCCTGCCC
CAGCGGCATGTGGACACAGGAATGGGCCTGGAAAGGCTGGTGGCTGTGCTGCAAGGCAAA
CACTCCACCTATGACACTGACCTCTTTTCCCCGCTGCTCAACGCCATACAGCAGGGCTGC
AGGGCACCCCCTTACTTGGGCCGAGTAGGGGTGGCAGACGAGGGGCGCACAGACACAGCG
TACCGCGTGGTGGCTGACCACATCCGCACACTCAGTGTCTGCATCTCTGATGGCGTCTTC
CCTGGGATGTCAGGTCCCCCGCTGGTTCTTCGTCGGATCCTGCGTCGAGCTGTGCGTTTC
TCCATGGAGATCTTAAAGGCACCACCTGGCTTCCTAGGCAGCCTGGTACCTGTAGTGGTG
GAGACACTGGGAGATGCTTATCCAGAACTGCAAAGGAACTCAGCCCAGATCGCCAACCTG
GTGTCAGAGGACGAGGCAGCCTTCCTGGCCTCCCTGGAGCGGGGTAGGCGGATCATTGAT
CGGACTCTGAGGACCCTGGGGCCTTCAGATATGTTCCCTGCTGAAGTGGCCTGGTCCTTG
TCACTGTGTGGAGACCTGGGACTCCCCTTGGACATGGTAGAGCTGATGCTGGAGGAGAAA
GGGGTCCAGCTAGACTCCGCTGGACTGGAGCGGTTGGCCCAAGAGGAGGCCCAGCACCGG
GCACGGCAGGCTGAGCCAGTTCAGAAGCAGGGATTGTGGCTTGATGTCCATGCGCTTGGG
GAGCTGCAGCGCCAAGGAGTGCCCCCAACTGACGACAGCCCCAAGTACAACTACTCCCTG
CGACCCAGCGGAAGTTATGAGTTCGGCACCTGTGAGGCCCAGGTGTTGCAACTGTATACA
GAGGACGGGACAGCAGTGGCCTCCGTGGGGAAAGGCCAGCGCTGTGGCCTCCTCTTGGAC
AGGACCAACTTCTACGCAGAACAGGGGGGCCAGGCTTCAGACCGTGGCTACCTGGTGCGG
GCAGGGCAAGAGGACGTGCTGTTCCCAGTAGCCCGGGCCCAGGTCTGTGGAGGTTTCATC
CTGCATGAGGCAGTAGCCCCTGAGTGCCTGCGGTTAGGGGACCAGGTGCAGCTGCATGTG
GATGAGGCCTGGCGTCTAGGCTGCATGGCGAAGCATACGGCCACCCACCTGCTGAACTGG
GCACTGAGGCAGACCCTGGGCCCTGGCACAGAGCAGCAGGGCTCCCATCTCAATCCTGAG
CAGCTGCGCTTGGATGTGACCACCCAGACCCCATTGACCCCAGAGCAGCTCCGGGCAGTG
GAGAACACTGTGCAGGAGGCCGTGGGGCAGGATGAGGCTGTGTACATGGAGGAGGTGCCC
CTGGCGCTCACTGCCCAGGTCCCTGGCCTGCGCTCTCTGGATGAGGTTTACCCAGACCCT
GTGCGGGTGGTATCAGTGGGGGTGCCCGTGGCCCATGCATTGGACCCAGCCTCCCAAGCC
GCACTGCAGACCTCTGTGGAGCTATGCTGTGGGACGCACCTGTTACGTACTGGGGCTGTA
GGGGACCTGGTTATCATCGGGGACCGCCAGCTTTCCAAGGGCACTACCCGCCTGCTGGCC
GTCACTGGGGAGCAGGCCCAGCAGGCCCGAGAGCTAGGCCAGAGCCTGGCCCAGGAAGTG
AAAGCGGCCACTGAGCGGCTGAGTCTGGGGAGCCGGGATGTGGCGGAGGCACTGAGGCTG
TCCAAGGACATAGGACGACTCATTGAAGCTGTGGAAACTGCTGTGATGCCCCAGTGGCAG
CGGCGGGAGCTGCTGGCCACAGTGAAGATGCTGCAGCGGCGTGCCAACACTGCCATCCGT
AAGCTGCAAATGGGACAGGCTGCAAAGAAAACTCAGGAGCTGCTGGAGCGGCACTCGAAG
GGGCCTCTGATTGTGGACACAGTCTCTGCTGAGTCTCTCTCAGTGCTGGTGAAGGTGGTA
CGGCAGCTGTGTGAGCAGGCCCCCAGCACGTCTGTGCTCCTACTCAGCCCCCAGCCCATG
GGGAAGGTGCTGTGTGCCTGTCAGGTGGCCCAGGGTGCCATGCCCACCTTCACAGCAGAG
GCCTGGGCACTGGCAGTGTGCAGCCACATGGGGGGCAAGGCGTGGGGCTCGCGAGTGGTG
GCCCAAGGCACCGGAAGCACTACTGACCTGGAAGCTGCCCTCAGTATAGCCCAAACCTAT
GCCCTCAGCCAGCTCTGA
|
| Enzyme 20 GenBank Gene ID |
NM_020745.2  |
| Enzyme 20 GeneCard ID |
AARS2  |
| Enzyme 20 GenAtlas ID |
AARS2  |
| Enzyme 20 HGNC ID |
HGNC:21022  |
| Enzyme 20 Chromosome Location |
6 |
| Enzyme 20 Locus |
6p21.1 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bonnefond L, Fender A, Rudinger-Thirion J, Giege R, Florentz C, Sissler M: Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry. 2005 Mar 29;44(12):4805-16. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |