Srr
entrez
303306
canonical
uniprot
Q76EQ0
canonical
ensembl
ENSRNOG00000002991
resolver
ensembl
ENSRNOG00055029610
resolver
ensembl
ENSRNOG00060030095
resolver
ensembl
ENSRNOG00065021256
resolver
ensp
ENSRNOP00000050774
resolver
ensp
ENSRNOP00055042248
resolver
ensp
ENSRNOP00060043543
resolver
ensp
ENSRNOP00065029141
resolver
enst
ENSRNOT00000046110
resolver
enst
ENSRNOT00055051280
resolver
enst
ENSRNOT00060052322
resolver
enst
ENSRNOT00065036151
resolver
genesymbol
Srr
resolver
uniprot_entry
SRR_RAT
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 (By similarity). Competitively inhibited by malonate (By similarity) (PubMed:20106978). {ECO:0000250|UniProtKB:Q9GZT4, ECO:0000250|UniProtKB:Q9QZX7, ECO:0000269|PubMed:20106978}.
uniprot
proteins
amino_acid_sequence
MCAQYCISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTLEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVKSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSLSWVKQAERPAP
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 (PubMed:16713567, PubMed:20106978). 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:16713567, ECO:0000269|PubMed:20106978}.
uniprot
proteins
mass_dalton
35693
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
12946565
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16713567
uniprot
proteins
pubmed
17880399
uniprot
proteins
pubmed
20106978
uniprot
proteins
sequence_length
333
uniprot
proteins