ID   A0A1D9LMV5_9NEIS        Unreviewed;       355 AA.
AC   A0A1D9LMV5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=BKX93_22740 {ECO:0000313|EMBL:AOZ52552.1};
OS   Chromobacterium vaccinii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=1108595 {ECO:0000313|EMBL:AOZ52552.1, ECO:0000313|Proteomes:UP000178776};
RN   [1] {ECO:0000313|EMBL:AOZ52552.1, ECO:0000313|Proteomes:UP000178776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21-1 {ECO:0000313|EMBL:AOZ52552.1,
RC   ECO:0000313|Proteomes:UP000178776};
RA   Sparks M.E., Blackburn M.B., Gundersen-Rindal D.E., Mitchell A., Farrar R.,
RA   Kuhar D.;
RT   "Chromobacterium muskegensis sp. nov., an insecticidal bacterium isolated
RT   from Sphagnum bogs.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; CP017707; AOZ52552.1; -; Genomic_DNA.
DR   RefSeq; WP_070981515.1; NZ_CP017707.1.
DR   AlphaFoldDB; A0A1D9LMV5; -.
DR   STRING; 1108595.BKX93_22740; -.
DR   GeneID; 68844016; -.
DR   KEGG; cvc:BKX93_22740; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000178776; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06827; PLPDE_III_AR_proteobact; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_01201; Ala_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; IPR029066; PLP-binding_barrel.
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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}.
FT   DOMAIN          232..355
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        33
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        253
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         33
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   355 AA;  38277 MW;  335C432C65573AF0 CRC64;
     MRPLIATIRL DHLRHNYLLA RAAHGGKTLA VLKANGYGHN AVRCAQALAD IADGFAVACL
     EEALQLRAAG VAAPILLLEG VFEAAELAEV ERHRLWLVVQ SESQLRMLEE ANPAEPFRVW
     LMLDSGMHRE GFLPQHYRAA WLRLRDSGKA ESIVKMTHFA RADEPAVSMT QAQIEAFDAA
     TAGLPGEESM ANSAGLLCHP RARRDWGRAG IVLYGANPLP AGYLQGDALK PVMRLSSRIF
     GVRELAAGEP IGYGSNFVTD RPTRVGLIAC GYADGYPRLA SSGSPVAVDG RRSRIIGRVS
     MDMITVDLSD LPEAGIGSEV ELWGDAVSVN EVAAAAGSIS YELLCNIKRA HFAFV
//