SRR_ORYSI
ID SRR_ORYSI Reviewed; 339 AA.
AC A2XWA9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 ORFNames=OsI_16936;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Catalyzes the synthesis of D-serine from L-serine. Has
CC dehydratase activity towards both L-serine and D-serine. {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 -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; CM000129; EAY95119.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XWA9; -.
DR SMR; A2XWA9; -.
DR STRING; 39946.A2XWA9; -.
DR EnsemblPlants; BGIOSGA014575-TA; BGIOSGA014575-PA; BGIOSGA014575.
DR Gramene; BGIOSGA014575-TA; BGIOSGA014575-PA; BGIOSGA014575.
DR HOGENOM; CLU_021152_4_2_1; -.
DR OMA; LIHPFDH; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IEA:EnsemblPlants.
DR GO; GO:0030378; F:serine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0070178; P:D-serine metabolic process; IEA:EnsemblPlants.
DR GO; GO:0006563; P:L-serine metabolic process; IEA:EnsemblPlants.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Isomerase; Lyase; Magnesium; Metal-binding;
KW Nucleotide-binding; Pyridoxal phosphate; Reference proteome;
KW S-nitrosylation.
FT CHAIN 1..339
FT /note="Serine racemase"
FT /id="PRO_0000420347"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246..247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 68
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 122
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 35597 MW; 71C28D4F16C23875 CRC64;
MGSRGGSGGD GAESHGYAAD IHSIREAQAR IAPYVHKTPV LSSTSIDAIV GKQLFFKCEC
FQKAGAFKIR GASNSIFALD DDEASKGVVT HSSGNHAAAV ALAAKLRGIP AYIVIPRNAP
ACKVDNVKRY GGHIIWSDVS IESRESVAKR VQEETGAILV HPFNNKNTIS GQGTVSLELL
EEVPEIDTII VPISGGGLIS GVALAAKAIN PSIRILAAEP KGADDSAQSK AAGKIITLPS
TNTIADGLRA FLGDLTWPVV RDLVDDIIVV DDNAIVDAMK MCYEMLKVAV EPSGAIGLAA
ALSDEFKQSS AWHESSKIGI IVSGGNVDLG VLWESLYKR
