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Database: UniProt/TrEMBL
Entry: G8M818_9BURK
LinkDB: G8M818_9BURK
Original site: G8M818_9BURK 
ID   G8M818_9BURK            Unreviewed;       356 AA.
AC   G8M818;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   28-FEB-2018, entry version 47.
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=BYI23_A010390 {ECO:0000313|EMBL:AET88877.1};
OS   Burkholderia sp. YI23.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1097668 {ECO:0000313|EMBL:AET88877.1, ECO:0000313|Proteomes:UP000006801};
RN   [1] {ECO:0000313|EMBL:AET88877.1, ECO:0000313|Proteomes:UP000006801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YI23 {ECO:0000313|EMBL:AET88877.1,
RC   ECO:0000313|Proteomes:UP000006801};
RX   PubMed=22275096; DOI=10.1128/JB.06479-11;
RA   Lim J.S., Choi B.S., Choi A.Y., Kim K.D., Kim D.I., Choi I.Y.,
RA   Ka J.O.;
RT   "Complete Genome Sequence of the Fenitrothion-Degrading Burkholderia
RT   sp. Strain YI23.";
RL   J. Bacteriol. 194:896-896(2012).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP003087; AET88877.1; -; Genomic_DNA.
DR   RefSeq; WP_014191105.1; NC_016589.1.
DR   ProteinModelPortal; G8M818; -.
DR   STRING; 1097668.BYI23_A010390; -.
DR   EnsemblBacteria; AET88877; AET88877; BYI23_A010390.
DR   KEGG; byi:BYI23_A010390; -.
DR   PATRIC; fig|1097668.3.peg.1152; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006801; 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   Gene3D; 2.40.37.10; -; 2.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006801};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006801}.
FT   DOMAIN      232    356       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   356 AA;  37792 MW;  0653D761AE4C06E0 CRC64;
     MPRPLSATIH TAALANNLAI ARKYAPKSKV WAVVKANAYG HGLARAFPGL RATDGFGLLD
     LEEAAKLREL GWAGPILLLE GFFRPTDIDV IDRYSLTTAV HCDEQLRMLE MARLSKPVNI
     QLKMNSGMNR LGYTPAKFRA AWERARAVHG VGQITLMTHF SDADGPRGIA HQLEAFERGA
     EGIAGARSLA NSAGVLWHPD AHFDWVRPGI MLYGASPSGV TADIASTGLK PAMTLQSELI
     AVQTVDAGSS IGYGSTFTAG ESMRIGVVAC GYADGYPRIA PEGTPVIVDG VRTKLVGRVS
     MDMLTVDLTP CPGAGIGSRV ELWGANLPVD DVASAAGTIG YELMCAIAQR VPVRAE
//
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