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Database: UniProt/TrEMBL
Entry: G8M9I3_9BURK
LinkDB: G8M9I3_9BURK
Original site: G8M9I3_9BURK 
ID   G8M9I3_9BURK            Unreviewed;       374 AA.
AC   G8M9I3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-SEP-2017, entry version 46.
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_A012820 {ECO:0000313|EMBL:AET89120.1};
OS   Burkholderia sp. YI23.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1097668 {ECO:0000313|EMBL:AET89120.1, ECO:0000313|Proteomes:UP000006801};
RN   [1] {ECO:0000313|EMBL:AET89120.1, ECO:0000313|Proteomes:UP000006801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YI23 {ECO:0000313|EMBL:AET89120.1,
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}.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01201}.
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DR   EMBL; CP003087; AET89120.1; -; Genomic_DNA.
DR   RefSeq; WP_014191345.1; NC_016589.1.
DR   ProteinModelPortal; G8M9I3; -.
DR   STRING; 1097668.BYI23_A012820; -.
DR   EnsemblBacteria; AET89120; AET89120; BYI23_A012820.
DR   KEGG; byi:BYI23_A012820; -.
DR   PATRIC; fig|1097668.3.peg.1415; -.
DR   eggNOG; ENOG41089U0; 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; -; 1.
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; 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.
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}.
FT   DOMAIN      247    374       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     47     47       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    270    270       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     141    141       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201}.
FT   MOD_RES      47     47       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   374 AA;  39617 MW;  1139C48181E8B326 CRC64;
     MSACADDLRE YRLLRPAWAE IDEGAIAANL AVARKLAGDA RIWFVCKGDG FGFGAAKVAR
     LADAAGVDGL CVGSPEEGMA IRAAGVTRDI LLFASTLPED AAHVAALGLT VTIQSMESLR
     AFVTAGVPVD AFIEIDPGFG RFGFLASQWP EAFSALAHQR TVRLKGIYTH LSSPGDDAIT
     ARQAGVFDAA LADARSAGFD DLETMLASSR VMIAHPELRY SAVDPGRLLY GALDAEWMAR
     VPLRPMLRAI RGRIIHVQEH PAGSMLGIGY AAPIRLERAV RVGVVPIGFG DGLNHVPPLG
     RVLIGGREAT IMGRRSLQHT VIDLSALPEA GVGSVVTFVG EDGGGFIGID ELADAVRVPV
     MELLPRVVRM LPQI
//
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