ID   BSR_VIBPA               Reviewed;         409 AA.
AC   Q87HG4;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Broad specificity amino-acid racemase {ECO:0000255|HAMAP-Rule:MF_02212};
DE            EC=5.1.1.10 {ECO:0000255|HAMAP-Rule:MF_02212};
DE   Flags: Precursor;
GN   OrderedLocusNames=VPA1001;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC       substrates. {ECO:0000255|HAMAP-Rule:MF_02212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid = a D-alpha-amino acid;
CC         Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871;
CC         EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:32557; Evidence={ECO:0000255|HAMAP-Rule:MF_02212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02212};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02212};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_02212}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02212}.
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DR   EMBL; BA000032; BAC62344.1; -; Genomic_DNA.
DR   RefSeq; NP_800511.1; NC_004605.1.
DR   RefSeq; WP_005480249.1; NC_004605.1.
DR   AlphaFoldDB; Q87HG4; -.
DR   SMR; Q87HG4; -.
DR   GeneID; 1191694; -.
DR   KEGG; vpa:VPA1001; -.
DR   PATRIC; fig|223926.6.peg.3932; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_6; -.
DR   Proteomes; UP000002493; Chromosome 2.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR   GO; GO:0047679; F:arginine racemase activity; IEA:RHEA.
DR   GO; GO:0018113; F:lysine racemase activity; IEA:RHEA.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06826; PLPDE_III_AR2; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_02212; Bsr_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR043698; Racemase_Bsr/Lyr.
DR   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Isomerase; Periplasm; Pyridoxal phosphate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   CHAIN           26..409
FT                   /note="Broad specificity amino-acid racemase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT                   /id="PRO_0000114594"
FT   ACT_SITE        76
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   MOD_RES         76
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT   DISULFID        72..98
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
SQ   SEQUENCE   409 AA;  44326 MW;  8BF46C9023224E8B CRC64;
     MRLKKTLLSI AIAAATFTPA MHSIAAPLQL QATLDQESQI QSSNTWLEID LGQFKQNIEQ
     FKSHMNDQTK ICAVMKADAY GNGIAGLMPT IIEQQIPCVA IASNAEAQVV RDSGFKGQLM
     RVRSAEIGEI EGALDLNVEE LIGTLDQAKA IAALSKKANK TVKVHLALND GGMGRNGIDM
     TTENGKKEAL AIAKQSGVEI VGIMTHFPNY NAEEVRAKLG SFKESSAWLI KEANLKREDI
     LLHVANSYTA LNVPEAQLDM VRPGGVLYGD LPTNLEYPSI VSFKTRVASL HHLPKNSTVG
     YDSSFTTTKE SVMANLPVGY SDGYPRKMGN TADVLINGQR AKVVGVTSMN TTMIDVSDIK
     GVKPGSEVVL FGNQKSQTIN AAEIEKNADV IFPELYTIWG TSNPRVYVK
//