ID   C3LM07_VIBCM            Unreviewed;       428 AA.
AC   C3LM07;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Broad specificity amino-acid racemase {ECO:0000256|HAMAP-Rule:MF_02212};
DE            EC=5.1.1.10 {ECO:0000256|HAMAP-Rule:MF_02212};
GN   OrderedLocusNames=VCM66_1267 {ECO:0000313|EMBL:ACP05583.1};
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112 {ECO:0000313|EMBL:ACP05583.1, ECO:0000313|Proteomes:UP000001217};
RN   [1] {ECO:0000313|EMBL:ACP05583.1, ECO:0000313|Proteomes:UP000001217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2 {ECO:0000313|EMBL:ACP05583.1,
RC   ECO:0000313|Proteomes:UP000001217};
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC       substrates. {ECO:0000256|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:0000256|HAMAP-
CC         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:0000256|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:0000256|HAMAP-Rule:MF_02212};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_02212, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC       ECO:0000256|HAMAP-Rule:MF_02212}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.
CC       {ECO:0000256|ARBA:ARBA00023456, ECO:0000256|HAMAP-Rule:MF_02212}.
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DR   EMBL; CP001233; ACP05583.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3LM07; -.
DR   KEGG; vcm:VCM66_1267; -.
DR   HOGENOM; CLU_028393_2_2_6; -.
DR   Proteomes; UP000001217; Chromosome I.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_02212};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02212};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_02212};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_02212};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_02212}.
FT   DOMAIN          299..427
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        95
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         95
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
FT   DISULFID        91..117
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02212"
SQ   SEQUENCE   428 AA;  46407 MW;  2FD8D39D89537530 CRC64;
     MEQPLLSRKK NVPSMITTGD IMHFKATLLS LSIAATLPSF SLSAAPLHID TALPDAAQIQ
     QSNSWLEISL GQFQSNIEQF KSHMNANTKI CAIMKADAYG NGIRGLMPTI IAQGIPCVGV
     ASNAEARAVR ESGFKGELIR VRSASLSEMS SALDLNIEEL IGTHQQALDL AELAKQSGKT
     LKVHIALNDG GMGRNGIDMT TEAGKKEAVS IATQPSLSVV GIMTHFPNYN ADEVRAKLAQ
     FKESSTWLMQ QANLKREEIT LHVANSYTAL NVPEAQLDMV RPGGVLFGDL PTNPEYPSIV
     SFKTRVSSLH HLPKDSTVGY DSTFTTSRDS VLANLPVGYS DGYPRKMGNK AEVLINGQRA
     KVVGVTSMNT TVVDVTEIKG VLPGQEVVLF GQQQKQSIAV SEMENNAELI FPELYTLWGT
     SNPRFYVK
//