ID   D5W8W2_PARAM            Unreviewed;       356 AA.
AC   D5W8W2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=BC1002_1793 {ECO:0000313|EMBL:ADG15857.1};
OS   Paraburkholderia atlantica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2654982 {ECO:0000313|EMBL:ADG15857.1, ECO:0000313|Proteomes:UP000002190};
RN   [1] {ECO:0000313|EMBL:ADG15857.1, ECO:0000313|Proteomes:UP000002190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE1002 {ECO:0000313|EMBL:ADG15857.1,
RC   ECO:0000313|Proteomes:UP000002190};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Martinez-Romero E., Hernandez M.A.R.,
RA   Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome 1 of Burkholderia sp. CCGE1002.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG15857.1, ECO:0000313|Proteomes:UP000002190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE1002 {ECO:0000313|EMBL:ADG15857.1,
RC   ECO:0000313|Proteomes:UP000002190};
RX   PubMed=23209196; DOI=10.1128/JB.01756-12;
RA   Ormeno-Orrillo E., Rogel M.A., Chueire L.M., Tiedje J.M.,
RA   Martinez-Romero E., Hungria M.;
RT   "Genome Sequences of Burkholderia sp. Strains CCGE1002 and H160, Isolated
RT   from Legume Nodules in Mexico and Brazil.";
RL   J. Bacteriol. 194:6927-6927(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; CP002013; ADG15857.1; -; Genomic_DNA.
DR   RefSeq; WP_013089723.1; NC_014117.1.
DR   AlphaFoldDB; D5W8W2; -.
DR   STRING; 640511.BC1002_1793; -.
DR   KEGG; bge:BC1002_1793; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_0_4; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002190; Chromosome 1.
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          232..356
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        253
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         301
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   356 AA;  38098 MW;  721254BDCBB308F7 CRC64;
     MPRPLSATIH TAALANNLAV ARRHAPKSKI WAVVKANAYG HGLARVFPGL RATDGFGLLD
     LEEAVKLREL GWAGPILLLE GFFRPTDIDV IDRYSLTTAL HSDEQLRMLE MARLSKPVNI
     QLKMNTGMNR LGYTVEKFRA AWERARACQG VGQITLMTHF SDADAERGIA HQMEAFERGA
     QGIAGARSLS NSAATLWHPE AHFDWVRPGI ILYGASPSGV TAAIDGTGLQ PAMTLASELI
     AVQTLGEGSS VGYGSTFTAR APMRIGVVAC GYADGYPRVA PEGTPVIVDG VRTRIVGRVS
     MDMLTVDLTP VPTANVGSRV ELWGTALPID NVAQACGTIG YELMCAVAPR VPVRAE
//