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Database: UniProt/TrEMBL
Entry: B5ZWC1_RHILW
LinkDB: B5ZWC1_RHILW
Original site: B5ZWC1_RHILW 
ID   B5ZWC1_RHILW            Unreviewed;       388 AA.
AC   B5ZWC1;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   22-NOV-2017, entry version 74.
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=Rleg2_1046 {ECO:0000313|EMBL:ACI54340.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI54340.1, ECO:0000313|Proteomes:UP000008330};
RN   [1] {ECO:0000313|Proteomes:UP000008330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304 {ECO:0000313|Proteomes:UP000008330};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Yates R., Ardley J., Tiwari R.P., O'Hara G., Howieson J., Brau L.,
RA   Reeve W.;
RT   "Complete sequence of chromosome of Rhizobium leguminosarum bv.
RT   trifolii WSM2304.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001191; ACI54340.1; -; Genomic_DNA.
DR   RefSeq; WP_012557160.1; NC_011369.1.
DR   ProteinModelPortal; B5ZWC1; -.
DR   STRING; 395492.Rleg2_1046; -.
DR   EnsemblBacteria; ACI54340; ACI54340; Rleg2_1046.
DR   GeneID; 34192599; -.
DR   KEGG; rlt:Rleg2_1046; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; DTGFNRL; -.
DR   BioCyc; RLEG395492:GJB3-1048-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008330; 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   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:UP000008330};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ACI54340.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      247    384       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     49     49       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     146    146       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     327    327       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      49     49       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   388 AA;  41888 MW;  E9E0CF2AFF55ABC0 CRC64;
     MTDFPIPFED DDLFASAGLR LTVDLTALTE NWRDMAQRSG AARAAAVVKA DAYGMGIEDA
     GEALYMAGAR DFFVATVDEG VTLRLYAPDA RIFVLSGIWP GTERRFFEND LVPVISSDEQ
     LAFWMAVLAD YGDYPCALHV DTGFNRLGLH MDDAIALADD VSRPASFAPV LVMSHLACGD
     EPSHAMNRQQ LESFRRVSAA YEGIDSSLAA SAGIFLGEDY HFDLTRPGIA LYGGEAVCGL
     ANPMRPVATA EARIIQVRSV EAGETVSYGR ALQLRRKSRL AIASAGYADG YMRGLSSGGV
     PLRQAVPQGG QGFIAGHKVP VAGRITMDLT IFDITDLPDN AVRAGDYVEL FGKNMPLDDV
     ARAAGTIGYE ILTSMGLRHE RRYVADEE
//
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