|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5283 |
| Enzyme 1 Name |
Dihydrolipoyl dehydrogenase, mitochondrial |
| Enzyme 1 Synonyms |
- Dihydrolipoamide dehydrogenase
- Glycine cleavage system L protein
|
| Enzyme 1 Gene Name |
DLD |
| Enzyme 1 Protein Sequence |
>Dihydrolipoyl dehydrogenase, mitochondrial
MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKA
AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNL
DKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNIL
IATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT
AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGK
AEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP
MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGK
FPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI
ARVCHAHPTLSEAFREANLAASFGKSINF
|
| Enzyme 1 Number of Residues |
509 |
| Enzyme 1 Molecular Weight |
54176.9 |
| Enzyme 1 Theoretical pI |
7.95 |
| Enzyme 1 GO Classification |
| Function |
- FAD or FADH2 binding
- adenyl nucleotide binding
- binding
- catalytic activity
- dihydrolipoyl dehydrogenase activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on NADH or NADPH
- oxidoreductase activity, acting on a sulfur group of donors, NAD or NADP as acceptor
- purine nucleoside binding
|
| Process |
- cell redox homeostasis
- cellular homeostasis
- cellular process
- metabolic process
- oxidation reduction
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 1 General Function |
Involved in oxidoreductase activity |
| Enzyme 1 Specific Function |
Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ [RN:R08550]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
91199540  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P09622  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
DLDH_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1530 bp
ATGCAGAGCTGGAGTCGTGTGTACTGCTCCTTGGCCAAGAGAGGCCATTTCAATCGAATA
TCTCATGGCCTACAGGGACTTTCTGCAGTGCCTCTGAGAACTTACGCAGATCAGCCGATT
GATGCTGATGTAACAGTTATAGGTTCTGGTCCTGGAGGATATGTTGCTGCTATTAAAGCT
GCCCAGTTAGGCTTCAAGACAGTCTGCATTGAGAAAAATGAAACACTTGGTGGAACATGC
TTGAATGTTGGTTGTATTCCTTCTAAGGCTTTATTGAACAACTCTCATTATTACCATATG
GCCCATGGAAAAGATTTTGCATCTAGAGGAATTGAAATGTCCGAAGTTCGCTTGAATTTA
GACAAGATGATGGAGCAGAAGAGTACTGCAGTAAAAGCTTTAACAGGTGGAATTGCCCAC
TTATTCAAACAGAATAAGGTTGTTCATGTCAATGGATATGGAAAGATAACTGGCAAAAAT
CAAGTCACTGCTACGAAAGCTGATGGCGGCACTCAGGTTATTGATACAAAGAACATTCTT
ATAGCCACGGGTTCAGAAGTTACTCCTTTTCCTGGAATCACGATAGATGAAGATACAATA
GTGTCATCTACAGGTGCTTTATCTTTAAAAAAAGTTCCAGAAAAGATGGTTGTTATTGGT
GCAGGAGTAATAGGTGTAGAATTGGGTTCAGTTTGGCAAAGACTTGGTGCAGATGTGACA
GCAGTTGAATTTTTAGGTCATGTAGGTGGAGTTGGAATTGATATGGAGATATCTAAAAAC
TTTCAACGCATCCTTCAAAAACAGGGGTTTAAATTTAAATTGAATACAAAGGTTACTGGT
GCTACCAAGAAGTCAGATGGAAAAATTGATGTTTCTATTGAAGCTGCTTCTGGTGGTAAA
GCTGAAGTTATCACTTGTGATGTACTCTTGGTTTGCATTGGCCGACGACCCTTTACTAAG
AATTTGGGACTAGAAGAGCTGGGAATTGAACTAGATCCCAGAGGTAGAATTCCAGTCAAT
ACCAGATTTCAAACTAAAATTCCAAATATCTATGCCATTGGTGATGTAGTTGCTGGTCCA
ATGCTGGCTCACAAAGCAGAGGATGAAGGCATTATCTGTGTTGAAGGAATGGCTGGTGGT
GCTGTGCACATTGACTACAATTGTGTGCCATCAGTGATTTACACACACCCTGAAGTTGCT
TGGGTTGGCAAATCAGAAGAGCAGTTGAAAGAAGAGGGTATTGAGTACAAAGTTGGGAAA
TTCCCATTTGCTGCTAACAGCAGAGCTAAGACAAATGCTGACACAGATGGCATGGTGAAG
ATCCTTGGGCAGAAATCGACAGACAGAGTACTGGGAGCACATATTCTTGGACCAGGTGCT
GGAGAAATGGTAAATGAAGCTGCTCTTGCTTTGGAATATGGAGCATCCTGTGAAGATATA
GCTAGAGTCTGTCATGCACATCCGACCTTATCAGAAGCTTTTAGAGAAGCAAATCTTGCT
GCGTCATTTGGCAAATCAATCAACTTTTGA
|
| Enzyme 1 GenBank Gene ID |
NM_000108.3  |
| Enzyme 1 GeneCard ID |
DLD  |
| Enzyme 1 GenAtlas ID |
DLD  |
| Enzyme 1 HGNC ID |
HGNC:2898  |
| Enzyme 1 Chromosome Location |
7 |
| Enzyme 1 Locus |
7q31-q32 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Otulakowski G, Robinson BH: Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases. J Biol Chem. 1987 Dec 25;262(36):17313-8. [PubMed
]
- Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS: Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1422-6. [PubMed
]
- Feigenbaum AS, Robinson BH: The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements. Genomics. 1993 Aug;17(2):376-81. [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
]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [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
]
- Johanning GL, Morris JI, Madhusudhan KT, Samols D, Patel MS: Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10964-8. [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
]
- Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT: Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol. 2005 Jul 15;350(3):543-52. [PubMed
]
- Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS: How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. J Biol Chem. 2006 Jan 6;281(1):648-55. Epub 2005 Nov 1. [PubMed
]
- Brautigam CA, Wynn RM, Chuang JL, Machius M, Tomchick DR, Chuang DT: Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. Structure. 2006 Mar;14(3):611-21. Epub 2006 Jan 26. [PubMed
]
- Liu TC, Kim H, Arizmendi C, Kitano A, Patel MS: Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5186-90. [PubMed
]
- Hong YS, Kerr DS, Craigen WJ, Tan J, Pan Y, Lusk M, Patel MS: Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency. Hum Mol Genet. 1996 Dec;5(12):1925-30. [PubMed
]
- Shaag A, Saada A, Berger I, Mandel H, Joseph A, Feigenbaum A, Elpeleg ON: Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews. Am J Med Genet. 1999 Jan 15;82(2):177-82. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5677 |
| Enzyme 2 Name |
2-oxoglutarate dehydrogenase, mitochondrial |
| Enzyme 2 Synonyms |
- 2-oxoglutarate dehydrogenase complex component E1
- OGDC-E1
- Alpha-ketoglutarate dehydrogenase
|
| Enzyme 2 Gene Name |
OGDH |
| Enzyme 2 Protein Sequence |
>2-oxoglutarate dehydrogenase, mitochondrial
MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEE
MYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNV
DKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDES
DLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFET
PGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSEN
GVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINR
VTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIV
YETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDP
EAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKY
AELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPR
SMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMA
FGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSL
SEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLP
HGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFH
VLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKR
LLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEH
KNQGYYDYVKPRLRTTISRAKPVWYAGRDPAAAPATGNKKTHLTELQRLLDTAFDLDVFK
NFS
|
| Enzyme 2 Number of Residues |
1023 |
| Enzyme 2 Molecular Weight |
115934.4 |
| Enzyme 2 Theoretical pI |
6.86 |
| Enzyme 2 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
- oxoglutarate dehydrogenase (succinyl-transferring) activity
- thiamin pyrophosphate binding
- vitamin binding
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity |
| Enzyme 2 Specific Function |
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components:2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2 [RN:R01700]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
37674435  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q02218  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ODO1_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>3072 bp
ATGTTTCATTTAAGGACTTGTGCTGCTAAGTTGAGGCCATTGACGGCTTCCCAGACTGTT
AAGACATTTTCACAAAACAGACCAGCAGCAGCTAGGACATTTCAACAGATTCGGTGCTAT
TCTGCACCTGTTGCTGCTGAGCCCTTTCTCAGTGGGACTAGTTCGAACTATGTGGAGGAG
ATGTACTGTGCTTGGCTGGAAAACCCCAAAAGTGTACATAAGTCATGGGACATTTTTTTT
CGCAACACGAATGCCGGAGCCCCACCGGGCACTGCCTACCAGAGTCCCCTTCCCCTGAGC
CGAGGCTCCCTGGCTGCTGTGGCCCATGCACAGTCCCTGGTAGAAGCACAGCCCAACGTG
GACAAGCTCGTGGAGGACCACCTGGCAGTGCAGTCGCTCATCAGGGCATATCAGATACGA
GGGCACCATGTAGCACAGCTGGACCCCCTGGGGATTTTGGATGCTGATCTGGACTCCTCC
GTGCCCGCTGACATTATCTCATCCACAGACAAACTTGGGTTCTATGGCCTGGATGAGTCT
GACCTCGACAAGGTCTTCCACTTGCCCACCACCACTTTCATCGGGGGACAGGAATCAGCA
CTTCCTCTGCGGGAGATCATCCGTCGGCTGGAGATGGCCTACTGCCAGCATATTGGGGTG
GAGTTCATGTTCATCAATGACCTGGAGCAGTGCCAGTGGATCCGGCAGAAGTTTGAGACC
CCTGGGATCATGCAGTTCACAAATGAGGAGAAACGGACCCTGCTGGCCAGGCTTGTGCGG
TCCACCAGGTTTGAGGAGTTCCTACAGCGGAAGTGGTCCTCTGAGAAGCGCTTTGGTCTA
GAAGGCTGCGAGGTACTGATCCCTGCCCTCAAGACCATCATTGACAAGTCTAGTGAGAAT
GGCGTGGACTACGTGATCATGGGCATGCCACACAGAGGGCGGCTGAACGTGCTTGCAAAT
GTCATCAGGAAGGAGCTGGAACAGATCTTCTGTCAATTCGATTCAAAGCTGGAGGCAGCT
GATGAGGGCTCCGGAGATGTGAAGTACCACCTGGGCATGTATCACCGCAGGATCAATCGT
GTCACCGACAGGAACATTACCTTGTCCTTGGTGGCCAACCCTTCCCACCTTGAGGCCGCT
GACCCCGTGGTGATGGGCAAGACCAAAGCCGAACAGTTTTACTGTGGCGACACTGAAGGG
AAAAAGGTCATGTCCATCCTGTTGCATGGGGATGCTGCATTTGCTGGCCAGGGCATTGTG
TACGAGACCTTCCACCTCAGCGACCTGCCATCCTACACAACTCATGGCACCGTGCACGTG
GTCGTCAACAACCAGATCGGCTTCACCACCGACCCTCGGATGGCCCGCTCCTCCCCCTAC
CCCACTGACGTGGCCCGAGTGGTGAATGCCCCCATTTTCCACGTGAACTCAGATGACCCC
GAGGCTGTCATGTACGTGTGCAAAGTGGCGGCCGAGTGGAGGAGCACCTTCCACAAGGAC
GTGGTTGTCGATTTGGTGTGTTACCGGCGCAACGGCCACAACGAGATGGATGAGCCCATG
TTCACGCAGCCGCTCATGTACAAGCAGATCCGCAAGCAGAAGCCTGTGTTACAGAAGTAC
GCTGAGCTGCTGGTGTCGCAGGGTGTGGTCAACCAGCCTGAGTATGAGGAGGAAATTTCC
AAGTATGATAAGATCTGTGAGGAAGCTTTTGCCAGATCTAAAGATGAGAAGATCTTGCAC
ATTAAGCACTGGCTGGACTCTCCCTGGCCTGGCTTCTTCACCCTGGACGGGCAGCCCAGG
AGCATGTCCTGCCCCTCCACGGGTCTGACGGAGGATATTCTGACACACATCGGGAATGTG
GCTAGTTCTGTGCCTGTGGAAAACTTTACTATTCATGGAGGGCTGAGCCGGATCTTGAAG
ACTCGTGGGGAAATGGTGAAGAACCGGACTGTGGACTGGGCTCTAGCGGAGTACATGGCG
TTTGGCTCGCTCCTGAAGGAGGGCATCCACATTCGGCTGAGCGGCCAGGACGTGGAGCGG
GGCACATTCAGCCACCGCCACCATGTGCTCCATGACCAGAATGTGGACAAGAGAACCTGC
ATCCCCATGAACCATCTCTGGCCCAATCAGGCCCCCTATACTGTGTGCAACAGCTCACTG
TCTGAGTACGGCGTGCTGGGCTTTGAGCTGGGCTTCGCCATGGCCAGTCCTAATGCCCTG
GTCCTCTGGGAAGCCCAATTTGGTGACTTCCACAACACGGCCCAGTGTATCATCGACCAG
TTCATCTGCCCGGGACAAGCCAAGTGGGTGCGGCAGAATGGCATCGTGTTGCTGCTGCCC
CATGGCATGGAGGGCATGGGTCCAGAACATTCCTCCGCCCGCCCAGAGCGGTTCTTGCAG
ATGTGCAACGATGACCCAGATGTCCTGCCAGACCTTAAAGAAGCCAACTTCGACATCAAT
CAGCTATATGACTGCAATTGGGTTGTTGTCAACTGCTCCACTCCTGGCAACTTCTTCCAC
GTGCTACGACGCCAGATCCTGCTGCCATTCCGGAAGCCGTTAATTATCTTCACCCCCAAA
TCCCTGTTGCGCCACCCCGAGGCCAGATCCAGCTTTGATGAGATGCTTCCAGGAACCCAC
TTCCAGCGGGTGATCCCAGAAGATGGCCCTGCAGCTCAGAACCCAGAAAATGTCAAAAGG
CTTCTCTTCTGCACCGGCAAAGTGTATTATGACCTCACCCGGGAGCGCAAAGCACGCGAC
ATGGTGGGGCAGGTGGCCATCACAAGGATTGAGCAGCTGTCGCCATTCCCCTTTGACCTC
CTGCTGAAGGAGGTGCAGAAGTACCCCAATGCTGAGCTGGCCTGGTGCCAGGAGGAGCAC
AAGAACCAAGGCTACTATGACTACGTGAAGCCAAGACTTCGGACCACCATCAGCCGCGCC
AAGCCCGTCTGGTATGCCGGCCGGGACCCAGCGGCTGCTCCAGCCACCGGCAACAAGAAG
ACCCACCTGACGGAGCTGCAGCGCCTCCTGGACACGGCCTTCGACCTGGACGTCTTCAAG
AACTTCTCGTAG
|
| Enzyme 2 GenBank Gene ID |
AC004859  |
| Enzyme 2 GeneCard ID |
OGDH  |
| Enzyme 2 GenAtlas ID |
OGDH  |
| Enzyme 2 HGNC ID |
HGNC:8124  |
| Enzyme 2 Chromosome Location |
7 |
| Enzyme 2 Locus |
7p14-p13 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Koike K, Urata Y, Goto S: Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide). Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1963-7. [PubMed
]
- Koike K: The gene encoding human 2-oxoglutarate dehydrogenase: structural organization and mapping to chromosome 7p13-p14. Gene. 1995 Jul 4;159(2):261-6. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [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
]
- Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D: Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. Proteomics. 2007 Mar;7(6):868-74. [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
]
- Jones LL, Colf LA, Bankovich AJ, Stone JD, Gao YG, Chan CM, Huang RH, Garcia KC, Kranz DM: Different thermodynamic binding mechanisms and peptide fine specificities associated with a panel of structurally similar high-affinity T cell receptors. Biochemistry. 2008 Nov 25;47(47):12398-408. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
8585 |
| Enzyme 3 Name |
Aminoadipate aminotransferase, isoform CRA_b |
| Enzyme 3 Synonyms |
- SubName: Putative uncharacterized protein AADAT
- SubName: cDNA, FLJ95590, Homo sapiens L-kynurenine/alpha-aminoadipate aminotransferase (KATII), mRNA
|
| Enzyme 3 Gene Name |
AADAT |
| Enzyme 3 Protein Sequence |
>Aminoadipate aminotransferase, isoform CRA_b
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
|
| Enzyme 3 Number of Residues |
425 |
| Enzyme 3 Molecular Weight |
47351.2 |
| Enzyme 3 Theoretical pI |
6.96 |
| Enzyme 3 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 3 General Function |
Transcription |
| Enzyme 3 Specific Function |
Not Available |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
63995206  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q4W5N8  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
Q4W5N8_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1278 bp
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGACTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTGGCTGGTGGCTTA
CCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAAAATGGAAAGACC
ATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCGAGTGCTGGAATT
CCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAATCCTCCTACCATC
CATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGCAGCCAACAAGGT
CTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTCCTAGATGAACCT
GCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATTATTAATGTTGCC
AGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCCAGATGGAAACCA
GAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACTGTTCCAAATGGC
AACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATCTATGAGCTTGCA
AGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTCCAGTTTAACAAG
TTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATCAGAGCTGACTCT
TTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGTCCAAAACCCTTA
ATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGCACTTTTAACCAG
CTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATGGCTCATGTAGAC
AGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCTGCAGACAAGTGG
TTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTATGGATTAAAGTT
AAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAGATGGGGGTATTA
ATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCTTACTTGAGAGCA
TCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTATTAGCACAACTT
ATAAAAGAATCTTTATGA
|
| Enzyme 3 GenBank Gene ID |
AC084866  |
| Enzyme 3 GeneCard ID |
AADAT  |
| Enzyme 3 GenAtlas ID |
Not Available |
| Enzyme 3 HGNC ID |
Not Available |
| Enzyme 3 Chromosome Location |
4 |
| Enzyme 3 Locus |
4q33 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
14844 |
| Enzyme 4 Name |
2-oxoglutarate dehydrogenase-like, mitochondrial |
| Enzyme 4 Synonyms |
- 2-oxoglutarate dehydrogenase complex component E1-like
- OGDC-E1-like
- Alpha-ketoglutarate dehydrogenase-like
|
| Enzyme 4 Gene Name |
OGDHL |
| Enzyme 4 Protein Sequence |
>2-oxoglutarate dehydrogenase-like, mitochondrial
MSQLRLLPSRLGVQAARLLAAHDVPVFGWRSRSSGPPATFPSSKGGGGSSYMEEMYFAWL
ENPQSVHKSWDSFFREASEEAFSGSAQPRPPSVVHESRSAVSSRTKTSKLVEDHLAVQSL
IRAYQIRGHHVAQLDPLGILDADLDSFVPSDLITTIDKLAFYDLQEADLDKEFQLPTTTF
IGGSENTLSLREIIRRLENTYCQHIGLEFMFINDVEQCQWIRQKFETPGVMQFSSEEKRT
LLARLVRSMRFEDFLARKWSSEKRFGLEGCEVMIPALKTIIDKSSEMGIENVILGMPHRG
RLNVLANVIRKDLEQIFCQFDPKLEAADEGSGDVKYHLGMYHERINRVTNRNITLSLVAN
PSHLEAVDPVVQGKTKAEQFYRGDAQGKKVMSILVHGDAAFAGQGVVYETFHLSDLPSYT
TNGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVIYVCSVAAEW
RNTFNKDVVVDLVCYRRRGHNEMDEPMFTQPLMYKQIHRQVPVLKKYADKLIAEGTVTLQ
EFEEEIAKYDRICEEAYGRSKDKKILHIKHWLDSPWPGFFNVDGEPKSMTCPATGIPEDM
LTHIGSVASSVPLEDFKIHTGLSRILRGRADMTKNRTVDWALAEYMAFGSLLKEGIHVRL
SGQDVERGTFSHRHHVLHDQEVDRRTCVPMNHLWPDQAPYTVCNSSLSEYGVLGFELGYA
MASPNALVLWEAQFGDFHNTAQCIIDQFISTGQAKWVRHNGIVLLLPHGMEGMGPEHSSA
RPERFLQMSNDDSDAYPAFTKDFEVSQLYDCNWIVVNCSTPANYFHVLRRQILLPFRKPL
IIFTPKSLLRHPEAKSSFDQMVSGTSFQRVIPEDGAAARAPEQVQRLIFCTGKVYYDLVK
ERSSQDLEEKVAITRLEQISPFPFDLIKQEAEKYPGAELAWCQEEHKNMGYYDYISPRFM
TILRRARPIWYVGRDPAAAPATGNRNTHLVSLKKFLDTAFNLQAFEGKTF
|
| Enzyme 4 Number of Residues |
1010 |
| Enzyme 4 Molecular Weight |
114480.3 |
| Enzyme 4 Theoretical pI |
6.63 |
| Enzyme 4 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
- oxoglutarate dehydrogenase (succinyl-transferring) activity
- thiamin pyrophosphate binding
- vitamin binding
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- glycolysis
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in oxoglutarate dehydrogenase (succinyl-transferring) activity |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
221316661  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9ULD0  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
OGDHL_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>3033 bp
ATGAGTCAGCTGAGGCTGCTGCCGTCCCGTCTTGGGGTACAGGCTGCGAGGCTCCTGGCT
GCACATGACGTCCCGGTGTTTGGCTGGCGCAGCAGGTCCTCCGGGCCACCGGCCACCTTC
CCAAGCAGCAAAGGTGGAGGCGGCTCCAGTTACATGGAGGAGATGTACTTCGCCTGGTTG
GAAAACCCCCAGAGTGTCCACAAGTCCTGGGACAGCTTCTTCAGGGAAGCCAGCGAGGAA
GCCTTTTCTGGCTCTGCTCAGCCACGGCCCCCTTCTGTTGTCCATGAGAGCAGGTCTGCA
GTCTCAAGTCGGACCAAGACCAGCAAATTGGTGGAGGACCACCTGGCTGTGCAGTCCCTG
ATCCGGGCCTACCAGATCCGGGGTCACCATGTGGCCCAGCTGGACCCCCTGGGCATTCTG
GATGCAGACCTGGACTCCTTTGTGCCCTCAGACTTGATCACAACCATTGATAAACTGGCC
TTCTATGACCTTCAGGAGGCTGACCTTGATAAGGAGTTCCAGCTGCCGACAACCACCTTC
ATTGGGGGCTCTGAAAACACCCTCTCTCTGCGGGAGATCATTCGGCGCCTGGAGAACACC
TACTGCCAGCACATTGGCCTGGAGTTCATGTTCATCAACGATGTGGAGCAGTGCCAGTGG
ATCCGGCAGAAGTTTGAGACCCCTGGTGTGATGCAGTTCTCCAGCGAGGAGAAGCGGACC
CTGCTGGCCCGGCTAGTGCGCTCCATGAGGTTTGAAGACTTCCTGGCCCGGAAATGGTCC
TCAGAGAAGCGGTTTGGCCTGGAGGGCTGTGAAGTGATGATTCCTGCCCTCAAGACCATC
ATCGACAAATCCAGCGAGATGGGGATTGAGAATGTCATCTTGGGGATGCCACACAGGGGA
AGGCTGAACGTGCTGGCCAACGTGATCCGCAAGGACCTGGAGCAGATCTTCTGCCAGTTT
GACCCCAAGCTGGAGGCGGCGGACGAGGGCTCCGGGGATGTCAAGTACCACCTGGGCATG
TACCATGAGAGGATCAACCGCGTCACCAACCGGAACATCACTCTGTCGCTGGTTGCCAAC
CCCTCCCACCTGGAGGCAGTGGACCCTGTGGTGCAGGGGAAGACAAAGGCAGAGCAGTTC
TACCGTGGAGATGCCCAGGGCAAGAAGGTCATGTCCATCCTGGTTCATGGGGACGCCGCC
TTTGCTGGCCAGGGCGTGGTATATGAGACCTTCCACCTGAGCGACCTGCCCTCCTACACG
ACCAATGGTACCGTGCACGTCGTCGTCAACAACCAGATTGGATTCACCACAGACCCCCGA
ATGGCCCGCTCCTCACCATACCCGACCGACGTGGCCCGGGTGGTCAATGCGCCTATCTTC
CATGTGAATGCCGATGACCCAGAGGCTGTGATATATGTGTGCAGTGTGGCAGCCGAATGG
AGAAACACTTTCAACAAAGATGTTGTCGTGGACCTGGTCTGTTACCGCCGGCGTGGCCAC
AATGAGATGGACGAGCCCATGTTCACCCAGCCGCTCATGTACAAGCAGATCCACAGACAG
GTGCCTGTGCTGAAGAAGTACGCAGACAAGCTGATTGCCGAGGGCACAGTCACCCTGCAG
GAGTTTGAGGAAGAAATTGCCAAATACGACCGGATCTGTGAGGAGGCTTATGGCAGGTCC
AAGGATAAAAAGATTCTGCATATAAAGCACTGGTTGGACTCCCCCTGGCCTGGCTTCTTC
AACGTAGATGGGGAGCCCAAGAGCATGACATGCCCAGCCACGGGGATCCCTGAGGACATG
CTCACCCACATCGGCAGTGTGGCCAGCTCTGTGCCCCTGGAGGACTTTAAGATCCACACT
GGCCTCTCTCGCATTCTGCGGGGCCGTGCGGACATGACCAAGAACCGGACGGTGGACTGG
GCGTTGGCAGAGTACATGGCCTTTGGCTCCCTGCTGAAGGAAGGCATCCACGTGCGGCTC
AGCGGGCAGGATGTGGAGAGGGGCACATTCAGTCACCGGCACCATGTTCTCCATGACCAG
GAGGTTGACCGCAGGACGTGTGTGCCTATGAATCATCTCTGGCCTGACCAGGCCCCGTAC
ACCGTGTGCAACAGCTCCCTCTCGGAGTACGGAGTCCTGGGCTTTGAGCTGGGCTATGCC
ATGGCCAGCCCCAATGCCCTGGTCCTCTGGGAGGCCCAGTTTGGGGACTTCCACAACACG
GCCCAGTGCATCATCGACCAGTTCATCAGCACCGGCCAGGCCAAGTGGGTGCGGCATAAT
GGCATTGTGCTGCTGCTGCCCCATGGCATGGAAGGCATGGGCCCAGAGCACTCGTCAGCG
AGGCCCGAAAGGTTCCTGCAGATGAGCAATGATGACTCGGATGCCTACCCTGCATTCACC
AAGGACTTCGAGGTGAGCCAGCTCTATGACTGCAACTGGATCGTGGTCAACTGCTCCACA
CCGGCCAACTACTTCCACGTGCTGCGCCGGCAGATCCTGCTGCCCTTCCGCAAGCCGCTG
ATTATCTTCACACCTAAATCTCTGCTGAGGCACCCAGAGGCCAAGTCCAGCTTTGACCAA
ATGGTATCCGGGACCAGCTTCCAGCGGGTGATTCCTGAAGATGGGGCCGCAGCACGGGCC
CCTGAGCAGGTGCAGCGGCTCATCTTCTGCACGGGAAAGGTGTACTATGACCTGGTGAAG
GAGCGGAGCAGCCAGGACCTGGAGGAGAAAGTGGCCATCACGCGCCTGGAGCAGATCTCT
CCATTCCCCTTCGACCTGATCAAGCAGGAGGCAGAGAAGTACCCAGGTGCGGAGCTGGCC
TGGTGTCAGGAGGAGCACAAGAACATGGGCTACTATGACTACATCAGCCCACGCTTCATG
ACCATCCTGAGGCGCGCACGGCCCATATGGTATGTTGGCCGGGACCCAGCGGCTGCACCA
GCCACAGGAAACAGGAACACTCACCTGGTGTCACTGAAGAAGTTTCTGGATACTGCCTTC
AATCTCCAGGCCTTTGAGGGCAAGACATTTTAG
|
| Enzyme 4 GenBank Gene ID |
NM_018245.2  |
| Enzyme 4 GeneCard ID |
OGDHL  |
| Enzyme 4 GenAtlas ID |
OGDHL  |
| Enzyme 4 HGNC ID |
HGNC:25590  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
10q11.23 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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
]
- 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 4 Metabolite References |
Not Available |
|
Enzyme 5
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|
| Enzyme 5 ID |
16512 |
| Enzyme 5 Name |
Putative uncharacterized protein |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
DLD |
| Enzyme 5 Protein Sequence |
>Putative uncharacterized protein
MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKA
AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNL
DKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNIL
IATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVT
AVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGK
AEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGP
MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGK
FPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI
ARVCHAHPTLSEAFREANLAASFGKSINF
|
| Enzyme 5 Number of Residues |
509 |
| Enzyme 5 Molecular Weight |
54178 |
| Enzyme 5 Theoretical pI |
7.95 |
| Enzyme 5 GO Classification |
| Function |
- FAD binding
- adenyl nucleotide binding
- binding
- catalytic activity
- dihydrolipoyl dehydrogenase activity
- disulfide oxidoreductase activity
- electron transporter activity
- nucleotide binding
- oxidoreductase activity
- purine nucleotide binding
- transporter activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 5 General Function |
Energy production and conversion |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| 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 |
B2R5X0  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
B2R5X0_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
Not Available |
| Enzyme 5 GenBank Gene ID |
AK312346  |
| Enzyme 5 GeneCard ID |
B2R5X0  |
| Enzyme 5 GenAtlas ID |
Not Available |
| Enzyme 5 HGNC ID |
Not Available |
| Enzyme 5 Chromosome Location |
Not Available |
| Enzyme 5 Locus |
Not Available |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |