ID   K0HVZ9_9BURK            Unreviewed;       371 AA.
AC   K0HVZ9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:AFU44015.1};
GN   ORFNames=C380_01445 {ECO:0000313|EMBL:AFU44015.1};
OS   Acidovorax sp. KKS102.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU44015.1, ECO:0000313|Proteomes:UP000006306};
RN   [1] {ECO:0000313|EMBL:AFU44015.1, ECO:0000313|Proteomes:UP000006306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KKS102 {ECO:0000313|EMBL:AFU44015.1,
RC   ECO:0000313|Proteomes:UP000006306};
RX   PubMed=23209225; DOI=10.1128/JB.01848-12;
RA   Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT   "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT   Polychlorinated-Biphenyl Degrader.";
RL   J. Bacteriol. 194:6970-6971(2012).
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, ECO:0000256|HAMAP-
CC         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; CP003872; AFU44015.1; -; Genomic_DNA.
DR   RefSeq; WP_015012110.1; NC_018708.1.
DR   AlphaFoldDB; K0HVZ9; -.
DR   STRING; 358220.C380_01445; -.
DR   KEGG; ack:C380_01445; -.
DR   PATRIC; fig|358220.3.peg.297; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_0_4; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006306; 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; IPR020622; Ala_racemase_pyridoxalP-BS.
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.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 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          235..368
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        256
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   371 AA;  39969 MW;  FD9067B79A7B82D0 CRC64;
     MPRPIAATIH TTALHHNLAR VRQSVPDAKV WAVVKANAYG HGIERVYEGL RGADGFALLD
     LAEAERVRHL GWRGPILLLE GVFEPRDLEL CSRLGLWHAV HCDEQIDMLA AHKTQVPHRV
     FLKMNSGMNR LGFTPERYRA AWARLNALPQ VDEISFMTHF SDADGPRGIA HQMAAFNAAA
     QDLPGERSLS NSAATLRHAQ DAGVRADWVR AGIVVYGSAP DFPEHHAGHW GLQPTMTLST
     RLIATQQLQA GDTVGYGSRF TADGPLTIGI AACGYADGYP RHCDTGTPVL VNGVRTRLVG
     RVSMDMVTVD LTPLQQAGVD VGFGSEVTLW GRASNGVVLS IDEVAQAAGT VGYELMCALA
     QRVPVVVDGG A
//