Serine racemase
Details
- Name
- Serine racemase
- Synonyms
- 5.1.1.18
- D-serine ammonia-lyase
- D-serine dehydratase
- L-serine ammonia-lyase
- L-serine dehydratase
- Gene Name
- SRR
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0016075|Serine racemase MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGA LNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQA YGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDAL VVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGV KSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQT VSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
- Number of residues
- 340
- Molecular Weight
- 36565.905
- Theoretical pI
- 6.51
- GO Classification
- FunctionsATP binding / calcium ion binding / D-serine ammonia-lyase activity / glycine binding / L-serine ammonia-lyase activity / magnesium ion binding / PDZ domain binding / protein homodimerization activity / pyridoxal phosphate binding / serine racemase activity / threonine racemase activityProcessesaging / brain development / D-serine biosynthetic process / D-serine metabolic process / L-serine metabolic process / protein homotetramerization / pyruvate biosynthetic process / response to drug / response to lipopolysaccharide / response to morphine / serine family amino acid metabolic processComponentsapical part of cell / cytoplasm / neuronal cell body / plasma membrane
- General Function
- Threonine racemase activity
- Specific Function
- Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.
- Pfam Domain Function
- PALP (PF00291)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0000772|1023 bp ATGTGTGCTCAGTATTGCATCTCCTTTGCTGATGTTGAAAAAGCTCATATCAACATTCGA GATTCTATCCACCTCACACCAGTGCTAACAAGCTCCATTTTGAATCAACTAACAGGGCGC AATCTTTTCTTCAAATGTGAACTCTTCCAGAAAACAGGATCTTTTAAGATTCGTGGTGCT CTCAATGCCGTCAGAAGCTTGGTTCCTGATGCTTTAGAAAGGAAGCCGAAAGCTGTTGTT ACTCACAGCAGTGGAAACCATGGCCAGGCTCTCACCTATGCTGCCAAATTGGAAGGAATT CCTGCTTATATTGTGGTGCCCCAGACAGCTCCAGACTGTAAAAAACTTGCAATACAAGCC TACGGAGCGTCAATTGTATACTGTGAACCTAGTGATGAGTCCAGAGAAAATGTTGCAAAA AGAGTTACAGAAGAAACAGAAGGCATCATGGTACATCCCAACCAGGAGCCTGCAGTGATA GCTGGACAAGGGACAATTGCCCTGGAAGTGCTGAACCAGGTTCCTTTGGTGGATGCACTG GTGGTACCTGTAGGTGGAGGAGGAATGCTTGCTGGAATAGCAATTACAGTTAAGGCTCTG AAACCTAGTGTGAAGGTATATGCTGCTGAACCCTCAAATGCAGATGACTGCTACCAGTCC AAGCTGAAGGGGAAACTGATGCCCAATCTTTATCCTCCAGAAACCATAGCAGATGGTGTC AAATCCAGCATTGGCTTGAACACCTGGCCTATTATCAGGGACCTTGTGGATGATATCTTC ACTGTCACAGAGGATGAAATTAAGTGTGCAACCCAGCTGGTGTGGGAGAGGATGAAACTA CTCATTGAACCTACAGCTGGTGTTGGAGTGGCTGCTGTGCTGTCTCAACATTTTCAAACT GTTTCCCCAGAAGTAAAGAACATTTGTATTGTGCTCAGTGGTGGAAATGTAGACTTAACC TCCTCCATAACTTGGGTGAAGCAGGCTGAAAGGCCAGCTTCTTATCAGTCTGTTTCTGTT TAA
- Chromosome Location
- Not Available
- Locus
- 17p13
- External Identifiers
Resource Link UniProtKB ID Q9GZT4 UniProtKB Entry Name SRR_HUMAN GenBank Protein ID 11034785 GenBank Gene ID AF169974 GenAtlas ID SRR HGNC ID HGNC:14398 - General References
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- Xia M, Liu Y, Figueroa DJ, Chiu CS, Wei N, Lawlor AM, Lu P, Sur C, Koblan KS, Connolly TM: Characterization and localization of a human serine racemase. Brain Res Mol Brain Res. 2004 Jun 18;125(1-2):96-104. [Article]
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- Smith MA, Mack V, Ebneth A, Moraes I, Felicetti B, Wood M, Schonfeld D, Mather O, Cesura A, Barker J: The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. J Biol Chem. 2010 Apr 23;285(17):12873-81. doi: 10.1074/jbc.M109.050062. Epub 2010 Jan 27. [Article]