Srr
entrez
27364
canonical
uniprot
Q9QZX7
canonical
ensembl
ENSMUSG00000001323
resolver
ensp
ENSMUSP00000067552
resolver
ensp
ENSMUSP00000113372
resolver
ensp
ENSMUSP00000169345
resolver
ensp
ENSMUSP00000169346
resolver
ensp
ENSMUSP00000169347
resolver
ensp
ENSMUSP00000169348
resolver
ensp
ENSMUSP00000169350
resolver
ensp
ENSMUSP00000169351
resolver
ensp
ENSMUSP00000169370
resolver
genesymbol
Srr
resolver
uniprot
Q401M7
resolver
uniprot
Q5SWE4
resolver
uniprot
Q5SWE5
resolver
uniprot
Q5SWE7
resolver
uniprot
Q8BT19
resolver
uniprot
Q8CD11
resolver
uniprot_entry
SRR_MOUSE
resolver
uniprot_sec
Q401M7
resolver
uniprot_sec
Q5SWE4
resolver
uniprot_sec
Q5SWE5
resolver
uniprot_sec
Q5SWE7
resolver
uniprot_sec
Q8BT19
resolver
uniprot_sec
Q8CD11
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 (PubMed:40259883). Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP (PubMed:12393813, PubMed:12515328). {ECO:0000269|PubMed:12393813, ECO:0000269|PubMed:12515328, ECO:0000269|PubMed:40259883}.
uniprot
proteins
amino_acid_sequence
MCAQYCISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVKSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSPEVKNVCIVLSGGNVDLTSLNWVGQAERPAPYQTVSV
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. 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. {ECO:0000269|PubMed:10557334, ECO:0000269|PubMed:12393813, ECO:0000269|PubMed:12515328, ECO:0000269|PubMed:15536068, ECO:0000269|PubMed:17293453, ECO:0000269|PubMed:40259883}.
uniprot
proteins
mass_dalton
36359
uniprot
proteins
mutagenesis
MUTAGEN 51; /note="K->A: Impairs ATP-binding inducing a 80% decrease in racemase activity."; /evidence="ECO:0000269|PubMed:17293453"; MUTAGEN 113; /note="C->S: Abolishes S-nitrosylation."; /evidence="ECO:0000269|PubMed:17293453
uniprot
proteins
post_translational_modification
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:0000269|PubMed:40259883}.; PTM: S-nitrosylated, leading to decrease the enzyme activity. {ECO:0000269|PubMed:17293453}.
uniprot
proteins
protein_family
Serine/threonine dehydratase family
uniprot
proteins
pubmed
10557334
uniprot
proteins
pubmed
12393813
uniprot
proteins
pubmed
12515328
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15536068
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17293453
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
35915065
uniprot
proteins
pubmed
40259883
uniprot
proteins
sequence_length
339
uniprot
proteins