ID   D6CKL8_THIA3            Unreviewed;       367 AA.
AC   D6CKL8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 78.
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=dadX {ECO:0000313|EMBL:CAZ87486.1};
GN   OrderedLocusNames=THI_0773 {ECO:0000313|EMBL:CAZ87486.1};
OS   Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ87486.1, ECO:0000313|Proteomes:UP000002372};
RN   [1] {ECO:0000313|Proteomes:UP000002372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22701 / CIP 110005 / 3As
RC   {ECO:0000313|Proteomes:UP000002372};
RX   PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA   Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA   Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA   Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA   Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA   Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA   Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA   Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT   "Structure, function, and evolution of the Thiomonas spp. genome.";
RL   PLoS Genet. 6:E1000859-E1000859(2010).
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; FP475956; CAZ87486.1; -; Genomic_DNA.
DR   RefSeq; WP_013104844.1; NZ_CTRL01000010.1.
DR   AlphaFoldDB; D6CKL8; -.
DR   KEGG; thi:THI_0773; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_0_4; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002372; 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}; Reference proteome {ECO:0000313|Proteomes:UP000002372}.
FT   DOMAIN          235..367
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   367 AA;  39331 MW;  D199E0FA28291FFF CRC64;
     MPRPISAVIH TAALSHNLLR VRQATPASKV WAVVKANAYG HGIARAYGAL RTADGFALLD
     LTEAEKLRAL GWVGPILLLE GCFAPEDLAL CERLNLWHVV HCREQIDWLA VHRGNRTHRV
     FLKMNTGMNR VGFSPEAYAA AWERLNALPQ VGEITHMTHF ACADEAGGID EALARFARGV
     GHLPGERTLS NSAAALVHGA DPRVASDWVR PGIALYGSSP TGLALDAAHW KLRPAMSLRS
     ELIDIQHIAA GECVGYGARF TAPRPMRIGV VACGYADGYP RVAPNGTPIV VDGVRTQLVG
     RVSMDMITVD LEPVFAAGNQ PMIGSPVLLW GQDAQAELSI DEVAAAAGTL GYELMCALAA
     RVPVRVE
//