ID   A0A096DEF2_9BURK        Unreviewed;       368 AA.
AC   A0A096DEF2; A0A0K6HT25; D0IWC0; D8DCZ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
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:MDH1332577.1};
GN   ORFNames=N5D63_00305 {ECO:0000313|EMBL:MDH1332577.1}, P608_18935
GN   {ECO:0000313|EMBL:KGH08099.1};
OS   Comamonas thiooxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=363952 {ECO:0000313|EMBL:MDH1332577.1, ECO:0000313|Proteomes:UP001161065};
RN   [1] {ECO:0000313|EMBL:KGH08099.1, ECO:0000313|Proteomes:UP000029549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF2 {ECO:0000313|EMBL:KGH08099.1,
RC   ECO:0000313|Proteomes:UP000029549};
RA   Liu L., Zhu W., Xia X., Xu B., Luo M., Wang G.;
RT   "High correlation between genotypes and phenotypes of environmental
RT   bacteria Comamonas testosteroni strains.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MDH1332577.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GD03832 {ECO:0000313|EMBL:MDH1332577.1};
RA   Diorio-Toth L.;
RT   "Intensive care unit water sources are persistently colonized with multi-
RT   drug resistant bacteria and are the site of extensive horizontal gene
RT   transfer of antibiotic resistance genes.";
RL   Submitted (SEP-2022) 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, 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MDH1332577.1}.
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DR   EMBL; AWTP01000128; KGH08099.1; -; Genomic_DNA.
DR   EMBL; JAOCEK010000001; MDH1332577.1; -; Genomic_DNA.
DR   RefSeq; WP_003070517.1; NZ_VTRK01000003.1.
DR   GeneID; 69557848; -.
DR   PATRIC; fig|285.48.peg.829; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000029549; Unassembled WGS sequence.
DR   Proteomes; UP001161065; Unassembled WGS sequence.
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..364
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   368 AA;  40295 MW;  7DD1D5B92559F268 CRC64;
     MPRPITATIH PEAVRHNLER VRQAVPDAKL WSVIKANAYG HGIENVFEGL RATDGFAMLD
     LDEAQRVRNL GWRGPILLLE GVFELRDLEI CSRLGIWHAV HCDEQIDWLA AHKTQVGHRV
     FLKMNSGMNR LGFTPERFRA AYARLNALPQ VDEISFMTHF SDADVEHGLD HQLRVFHETT
     LDLPGERSVS NSAATLLHGD ENNVRCDWVR PGIVLYGSSP DFPTHDAAHW GLEPTMTLSS
     KIIGTQELHA GDTVGYGSRF QCDGPLRLGV VACGYADGYP RVCPTGTPVL VDGVRTRTLG
     RVSMDMMAVD LSPVPKARLG SEVTLWGRAS NGAVLPIDEV AAAAGTLGYE LMCAVAPRVP
     KQVEGAGK
//