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Database: UniProt/TrEMBL
Entry: A0A0A8GAE3_RHIET
LinkDB: A0A0A8GAE3_RHIET
Original site: A0A0A8GAE3_RHIET 
ID   A0A0A8GAE3_RHIET        Unreviewed;       389 AA.
AC   A0A0A8GAE3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   07-JUN-2017, entry version 17.
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:AJC78677.1};
GN   ORFNames=IE4803_CH01443 {ECO:0000313|EMBL:AJC78677.1};
OS   Rhizobium etli bv. phaseoli str. IE4803.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1432049 {ECO:0000313|EMBL:AJC78677.1, ECO:0000313|Proteomes:UP000031160};
RN   [1] {ECO:0000313|EMBL:AJC78677.1, ECO:0000313|Proteomes:UP000031160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IE4803 {ECO:0000313|EMBL:AJC78677.1,
RC   ECO:0000313|Proteomes:UP000031160};
RA   Bustos P., Santamaria R.I., Lozano L., Ormeno-Orrillo E., Rogel M.A.,
RA   Romero D., Cevallos M.A., Martinez-Romero E., Gonzalez V.;
RT   "Complete genome sequence of Rhizobium etli bv. phaseoli IE4803.";
RL   Submitted (MAY-2014) 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, 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; CP007641; AJC78677.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJC78677; AJC78677; IE4803_CH01443.
DR   KEGG; rep:IE4803_CH01443; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000031160; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
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; 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:UP000031160};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AJC78677.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      249    386       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     51     51       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     148    148       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     329    329       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      51     51       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   389 AA;  41977 MW;  31E4474371216AD3 CRC64;
     MWIMSEFLDV PEDDTFASAG LRLTVDLTAL TENWRDMAHR SGAARAAAVV KADAYGLGIE
     DAGEALYTAG ARDFFVATVD EGVTLRLYAP DARIFVLSGI WPGTERRFFD NDLVPVISSD
     QQLAFWMAVL ADYGDYPCAL HVDTGFNRLG LHIDDAIALA DDVSRPASFA PVLVMSHLAC
     GDDPTHVMNR QQLESFRRVT AAYEGIDSSL AASAGIFLGE DYHFDLTRPG IALYGGEAVC
     GMANPMRPVA TAEARIIQVR TVGAGETVSY GRALQLPRDS RLAIVSAGYA DGYMRSQSSG
     GVPLRQAVPQ GGQGFIAGHK VPVAGRITMD LTIFDVTDLP ENAVRAGDYV ELFGKNMPLD
     DVARAAGTIG YEILTSMGLR HERRYVAEE
//
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