|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6132 |
| Enzyme 1 Name |
Phosphoserine aminotransferase |
| Enzyme 1 Synonyms |
- Phosphohydroxythreonine aminotransferase
- PSAT
|
| Enzyme 1 Gene Name |
PSAT1 |
| Enzyme 1 Protein Sequence |
>Phosphoserine aminotransferase
MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLV
RELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGT
INIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSN
FLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLY
NTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVCPVEPQNRSK
MNIPFRIGNAKGDDALEKRFLDKALELNMLSLKGHRSVGGIRASLYNAVTIEDVQKLAAF
MKKFLEMHQL
|
| Enzyme 1 Number of Residues |
370 |
| Enzyme 1 Molecular Weight |
40422.4 |
| Enzyme 1 Theoretical pI |
7.77 |
| Enzyme 1 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
- L-serine biosynthetic process
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in metabolic process |
| Enzyme 1 Specific Function |
Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine |
| Enzyme 1 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Vitamin B6 Metabolism (map00750
)
|
| Enzyme 1 Reactions |
- (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate [RN:R04173]
- (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
17402893  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9Y617  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
SERC_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1113 bp
ATGGACGCCCCCAGGCAGGTGGTCAACTTTGGGCCTGGTCCCGCCAAGCTGCCGCACTCA
GTGTTGTTAGAGATACAAAAGGAATTATTAGACTACAAAGGAGTTGGCATTAGTGTTCTT
GAAATGAGTCACAGGTCATCAGATTTTGCCAAGATTATTAACAATACAGAGAATCTTGTG
CGGGAATTGCTAGCTGTTCCAGACAACTATAAGGTGATTTTTCTGCAAGGAGGTGGGTGC
GGCCAGTTCAGTGCTGTCCCCTTAAACCTCATTGGCTTGAAAGCAGGAAGGTGTGCTGAC
TATGTGGTGACAGGAGCTTGGTCAGCTAAGGCCGCAGAAGAAGCCAAGAAGTTTGGGACT
ATAAATATCGTTCACCCTAAACTTGGGAGTTATACAAAAATTCCAGATCCAAGCACCTGG
AACCTCAACCCAGATGCCTCCTACGTGTATTATTGCGCAAATGAGACGGTGCATGGTGTG
GAGTTTGACTTTATACCCGATGTCAAGGGAGCAGTACTGGTTTGTGACATGTCCTCAAAC
TTCCTGTCCAAGCCAGTGGATGTTTCCAAGTTTGGTGTGATTTTTGCTGGTGCCCAGAAG
AATGTTGGCTCTGCTGGGGTCACCGTGGTGATTGTCCGTGATGACCTGCTGGGGTTTGCC
CTCCGAGAGTGCCCCTCGGTCCTGGAATACAAGGTGCAGGCTGGAAACAGCTCCTTGTAC
AACACGCCTCCATGTTTCAGCATCTACGTCATGGGCTTGGTTCTGGAGTGGATTAAAAAC
AATGGAGGTGCCGCGGCCATGGAGAAGCTTAGCTCCATCAAATCTCAAACAATTTATGAG
ATTATTGATAATTCTCAAGGATTCTACGTTTGTCCAGTGGAGCCCCAAAATAGAAGCAAG
ATGAATATTCCATTCCGCATTGGCAATGCCAAAGGAGATGATGCTTTAGAAAAAAGATTT
CTTGATAAAGCTCTTGAACTCAATATGTTGTCCTTGAAAGGGCATAGGTCTGTGGGAGGC
ATCCGGGCCTCTCTGTATAATGCTGTCACAATTGAAGACGTTCAGAAGCTGGCCGCCTTC
ATGAAAAAATTTTTGGAGATGCATCAGCTATGA
|
| Enzyme 1 GenBank Gene ID |
NM_058179.2  |
| Enzyme 1 GeneCard ID |
PSAT1  |
| Enzyme 1 GenAtlas ID |
PSAT1  |
| Enzyme 1 HGNC ID |
HGNC:19129  |
| Enzyme 1 Chromosome Location |
9 |
| Enzyme 1 Locus |
9q21.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Baek JY, Jun DY, Taub D, Kim YH: Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis. Biochem J. 2003 Jul 1;373(Pt 1):191-200. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [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
]
- 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
]
- 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
]
- Hart CE, Race V, Achouri Y, Wiame E, Sharrard M, Olpin SE, Watkinson J, Bonham JR, Jaeken J, Matthijs G, Van Schaftingen E: Phosphoserine aminotransferase deficiency: a novel disorder of the serine biosynthesis pathway. Am J Hum Genet. 2007 May;80(5):931-7. Epub 2007 Mar 30. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6169 |
| Enzyme 2 Name |
Phosphoserine phosphatase |
| Enzyme 2 Synonyms |
- PSP
- PSPase
- L-3-phosphoserine phosphatase
- O-phosphoserine phosphohydrolase
|
| Enzyme 2 Gene Name |
PSPH |
| Enzyme 2 Protein Sequence |
>Phosphoserine phosphatase
MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKA
ALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA
SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDG
ATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
|
| Enzyme 2 Number of Residues |
225 |
| Enzyme 2 Molecular Weight |
25007.5 |
| Enzyme 2 Theoretical pI |
5.42 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
- phosphoserine phosphatase activity
|
| Process |
- L-serine biosynthetic process
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in catalytic activity |
| Enzyme 2 Specific Function |
Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates |
| Enzyme 2 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 2 Reactions |
- O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate [RN:R00582 R02853]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
1890331  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P78330  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SERB_HUMAN  |
| Enzyme 2 PDB ID |
1NNL  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>678 bp
ATGGTCTCCCACTCAGAGCTGAGGAAGCTTTTCTACTCAGCAGATGCTGTGTGTTTTGAT
GTTGACAGCACGGTCATCAGAGAAGAAGGAATCGATGAGCTAGCCAAAATCTGTGGCGTT
GAGGACGCGGTGTCAGAAATGACACGGCGAGCCATGGGCGGGGCAGTGCCTTTCAAAGCT
GCTCTCACAGAGCGCTTAGCCCTCATCCAGCCCTCCAGGGAGCAGGTGCAGAGACTCATA
GCAGAGCAACCCCCACACCTGACCCCCGGCATAAGGGAGCTGGTAAGTCGCCTACAGGAG
CGAAATGTTCAGGTTTTCCTAATATCTGGTGGCTTTAGGAGTATTGTAGAGCATGTTGCT
TCAAAGCTCAATATCCCAGCAACCAATGTATTTGCCAATAGGCTGAAATTCTACTTTAAC
GGTGAATATGCAGGTTTTGATGAGACGCAGCCAACAGCTGAATCTGGTGGAAAAGGAAAA
GTGATTAAACTTTTAAAGGAAAAATTTCATTTTAAGAAAATAATCATGATTGGAGATGGT
GCCACAGATATGGAAGCCTGTCCTCCTGCTGATGCTTTCATTGGATTTGGAGGAAATGTG
ATCAGGCAACAAGTCAAGGATAACGCCAAATGGTATATCACTGATTTTGTAGAGCTGCTG
GGAGAACTGGAAGAATAA
|
| Enzyme 2 GenBank Gene ID |
Y10275  |
| Enzyme 2 GeneCard ID |
PSPH  |
| Enzyme 2 GenAtlas ID |
PSPH  |
| Enzyme 2 HGNC ID |
HGNC:9577  |
| Enzyme 2 Chromosome Location |
7 |
| Enzyme 2 Locus |
7p11.2 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Collet JF, Gerin I, Rider MH, Veiga-da-Cunha M, Van Schaftingen E: Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate. FEBS Lett. 1997 May 26;408(3):281-4. [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
]
- 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
]
- 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
]
- Veiga-da-Cunha M, Collet JF, Prieur B, Jaeken J, Peeraer Y, Rabbijns A, Van Schaftingen E: Mutations responsible for 3-phosphoserine phosphatase deficiency. Eur J Hum Genet. 2004 Feb;12(2):163-6. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
13053 |
| Enzyme 3 Name |
Phosphoserine aminotransferase 1 |
| Enzyme 3 Synonyms |
- Phosphoserine aminotransferase 1, isoform CRA_a
|
| Enzyme 3 Gene Name |
PSAT1 |
| Enzyme 3 Protein Sequence |
>Phosphoserine aminotransferase 1
MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLV
RELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGT
INIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSN
FLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLY
NTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVSVGGIRASLY
NAVTIEDVQKLAAFMKKFLEMHQL
|
| Enzyme 3 Number of Residues |
324 |
| Enzyme 3 Molecular Weight |
35189 |
| Enzyme 3 Theoretical pI |
6.66 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- L-serine biosynthesis
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 3 General Function |
Coenzyme transport and metabolism |
| 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 |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q5T7G5  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
Q5T7G5_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
Not Available |
| Enzyme 3 GenBank Gene ID |
AL353594  |
| Enzyme 3 GeneCard ID |
Q5T7G5  |
| Enzyme 3 GenAtlas ID |
PSAT1  |
| Enzyme 3 HGNC ID |
HGNC:19129  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
Not Available |
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
16507 |
| Enzyme 4 Name |
cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a) |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
PSPH |
| Enzyme 4 Protein Sequence |
>cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a)
MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKA
ALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA
SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDG
ATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
|
| Enzyme 4 Number of Residues |
225 |
| Enzyme 4 Molecular Weight |
25008 |
| Enzyme 4 Theoretical pI |
5.42 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
- phosphoserine phosphatase activity
|
| Process |
- L-serine biosynthesis
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| 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 |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
B2RCR5  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
B2RCR5_HUMAN  |
| Enzyme 4 PDB ID |
1NNL  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK315235  |
| Enzyme 4 GeneCard ID |
B2RCR5  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |