BSR_VIBVU
ID BSR_VIBVU Reviewed; 408 AA.
AC Q8D6Q0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 Name=alr; OrderedLocusNames=VV2_0478;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016796; AAO07429.1; -; Genomic_DNA.
DR RefSeq; WP_011081429.1; NC_004460.2.
DR AlphaFoldDB; Q8D6Q0; -.
DR SMR; Q8D6Q0; -.
DR EnsemblBacteria; AAO07429; AAO07429; VV2_0478.
DR KEGG; vvu:VV2_0478; -.
DR HOGENOM; CLU_028393_2_2_6; -.
DR OMA; TSMNTVM; -.
DR Proteomes; UP000002275; 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; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT CHAIN 25..408
FT /note="Broad specificity amino-acid racemase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT /id="PRO_0000114596"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT MOD_RES 75
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT DISULFID 71..97
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
SQ SEQUENCE 408 AA; 44106 MW; 3D8A964B40B670F4 CRC64;
MNFKKTLLSI AIASASLTPA FSYSAPLLLD NTVHQTSQIA GANAWLEISL GQFKSNIEQF
KSHIAPQTKI CAVMKADAYG NGIRGLMPTI LEQQIPCVAI ASNAEAKLVR ESGFEGELIR
VRSASTSEIE QALSLDIEEL IGSEQQAREL ASLAEKYSKT IKVHLALNDG GMGRNGIDMS
TERGPKEAVA IATHPSVAVV GIMTHFPNYN AEDVRTKLKS FNQHAQWLME SAGLKREEIT
LHVANSYTAL NVPEAQLDMV RPGGVLYGDL PTNPEYPSIV AFKTRVASLH SLPAGSTVGY
DSTFTTANDA VMANLTVGYS DGYPRKMGNK AQVLINGQRA NVVGVASMNT TMVDVSNIKG
VLPGDEVTLF GAQKNQHISV GEMEENAEVI FPELYTIWGT SNPRFYVK
