SRR
entrez
63826
canonical
uniprot
Q9GZT4
canonical
ensembl
ENSG00000167720
resolver
ensp
ENSP00000339435
resolver
ensp
ENSP00000458814
resolver
ensp
ENSP00000461482
resolver
ensp
ENSP00000579691
resolver
ensp
ENSP00000579692
resolver
ensp
ENSP00000579693
resolver
ensp
ENSP00000617805
resolver
enst
ENST00000344595
resolver
enst
ENST00000572709
resolver
enst
ENST00000574229
resolver
enst
ENST00000909632
resolver
enst
ENST00000909633
resolver
enst
ENST00000909634
resolver
enst
ENST00000947746
resolver
genesymbol
SRR
resolver
hgnc
HGNC:14398
resolver
uniprot
D3DTI5
resolver
uniprot
I3L4S4
resolver
uniprot
Q3ZK31
resolver
uniprot
Q6IA55
resolver
uniprot_entry
I3L4S4_HUMAN
resolver
uniprot_entry
Q3ZK31_HUMAN
resolver
uniprot_entry
SRR_HUMAN
resolver
uniprot_sec
D3DTI5
resolver
uniprot_sec
Q6IA55
resolver
activity_regulation
ACTIVITY REGULATION: Undergoes a suicide substrate reaction-like modification when incubated with L- or D-serine, resulting in a change in reaction specificity. The alpha-aminoacrylate intermediate can attack enzyme's active-site lysine residue, forming a covalent lysinoalanine bond. This self-modification decreases serine racemase activity and L-serine dehydratase activity, but it increases the dehydration activity toward D-Ser (By similarity). Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP. Competitively inhibited by malonate. Inhibited by meso-tartrate and malonate (PubMed:20106978, PubMed:23391306). {ECO:0000250|UniProtKB:Q9QZX7, ECO:0000269|PubMed:20106978, ECO:0000269|PubMed:23391306}.
uniprot
proteins
amino_acid_sequence
MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
uniprot
proteins
ec_number
4.3.1.17
uniprot
proteins
ec_number
4.3.1.18
uniprot
proteins
ec_number
5.1.1.18
uniprot
proteins
function
FUNCTION: Pyridoxal-5'-phosphate (PLP)-dependent enzyme that catalyzes the synthesis of D-serine from L-serine (PubMed:20106978, PubMed:23391306, PubMed:29277459). D-serine is a key coagonist with glutamate at NMDA receptors. In addition to racemization, has dehydratase activity towards both L-serine and D-serine, a two-step reaction in which the hydroxyl group of serine is eliminated to produce aminoacrylate (2-aminoprop-2-enoate), and then the aminoacrylate (an unstable intermediate) is deaminated by nonenzymatic hydrolysis to produce pyruvate (By similarity). {ECO:0000250|UniProtKB:Q9QZX7, ECO:0000269|PubMed:20106978, ECO:0000269|PubMed:23391306, ECO:0000269|PubMed:29277459}.
uniprot
proteins
mass_dalton
36566
uniprot
proteins
post_translational_modification
PTM: S-nitrosylated, leading to decrease the enzyme activity. {ECO:0000250|UniProtKB:Q9QZX7}.; PTM: Active site lysine residue becomes modified via an alpha-aminoacrylate intermediate derived from L-Ser, converting that lysine into a lysinoalanine residue. This modification changes the enzyme's properties. {ECO:0000250|UniProtKB:Q9QZX7}.
uniprot
proteins
protein_family
Serine/threonine dehydratase family
uniprot
proteins
pubmed
11054547
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15193426
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17880399
uniprot
proteins
pubmed
20106978
uniprot
proteins
pubmed
23391306
uniprot
proteins
pubmed
24138986
uniprot
proteins
pubmed
29277459
uniprot
proteins
pubmed
32039887
uniprot
proteins
pubmed
35410329
uniprot
proteins
sequence_length
340
uniprot
proteins