BSR_VIBPA
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 03-AUG-2022, entry version 106.
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; Proteobacteria; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 STRING; 223926.28809302; -.
DR EnsemblBacteria; BAC62344; BAC62344; BAC62344.
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 OMA; HAVEMVH; -.
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; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 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 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; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR00492; alr; 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
