SRR_BOVIN
ID SRR_BOVIN Reviewed; 334 AA.
AC A0JNI4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Serine racemase;
DE EC=4.3.1.17;
DE EC=4.3.1.18;
DE EC=5.1.1.18;
DE AltName: Full=D-serine ammonia-lyase;
DE AltName: Full=D-serine dehydratase;
DE AltName: Full=L-serine ammonia-lyase;
DE AltName: Full=L-serine dehydratase;
GN Name=SRR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of D-serine from L-serine. D-serine
CC is a key coagonist with glutamate at NMDA receptors. Has dehydratase
CC activity towards both L-serine and D-serine (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; EC=5.1.1.18;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosterically activated by magnesium, and
CC possibly also other divalent metal cations. Allosterically activated by
CC ATP, ADP or GTP (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- PTM: S-nitrosylated, leading to decrease the enzyme activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; BC126700; AAI26701.1; -; mRNA.
DR RefSeq; NP_001071433.1; NM_001077965.2.
DR RefSeq; XP_010814138.1; XM_010815836.2.
DR RefSeq; XP_010814140.1; XM_010815838.2.
DR AlphaFoldDB; A0JNI4; -.
DR SMR; A0JNI4; -.
DR STRING; 9913.ENSBTAP00000005532; -.
DR PaxDb; A0JNI4; -.
DR Ensembl; ENSBTAT00000005532; ENSBTAP00000005532; ENSBTAG00000004223.
DR GeneID; 525340; -.
DR KEGG; bta:525340; -.
DR CTD; 63826; -.
DR VEuPathDB; HostDB:ENSBTAG00000004223; -.
DR VGNC; VGNC:35292; SRR.
DR eggNOG; KOG1251; Eukaryota.
DR GeneTree; ENSGT00550000075026; -.
DR HOGENOM; CLU_021152_4_2_1; -.
DR InParanoid; A0JNI4; -.
DR OMA; LIHPFDH; -.
DR OrthoDB; 943371at2759; -.
DR TreeFam; TF313346; -.
DR Reactome; R-BTA-977347; Serine biosynthesis.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000004223; Expressed in semen and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016594; F:glycine binding; IEA:Ensembl.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0030378; F:serine racemase activity; ISS:UniProtKB.
DR GO; GO:0018114; F:threonine racemase activity; IBA:GO_Central.
DR GO; GO:0070179; P:D-serine biosynthetic process; IBA:GO_Central.
DR GO; GO:0070178; P:D-serine metabolic process; ISS:UniProtKB.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; ATP-binding; Isomerase; Lyase; Magnesium; Metal-binding;
KW Nucleotide-binding; Pyridoxal phosphate; Reference proteome;
KW S-nitrosylation.
FT CHAIN 1..334
FT /note="Serine racemase"
FT /id="PRO_0000286172"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 238..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 113
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZX7"
SQ SEQUENCE 334 AA; 36181 MW; 63277FE33D8FA45F CRC64;
MCDQYCISFA DVEKAHINIR DFIHLTPVLT SSILNQITGR NLFFKCELFQ KTGSFKIRGA
LNAIRGLISA HPEEKPRAVV AHSSGNHGQA LSFAARLEGI PAYVIVPETA PNCKKLAIQA
YGASIVYSEQ SEESRENITK RIAEETEGIM VHPNQEPAVI AGQGTIAMEV LNQVPLVDAL
VVPVGGGGML AGIAVTVKAL RPSVKVYAAE PLNADDCYQS KLKGELTPNP YPPETIADGI
KSSIGLNTWP IIRDLVDDVF TVTEDEIKYA TQLVWERMKL LIEPTAGVGV AVVLSQHFRT
VPAEVKNICI VLSGGNVDLT SLTWVKKQDE KAAP
