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Database: UniProt/TrEMBL
Entry: A0A0A8GMF6_RHIET
LinkDB: A0A0A8GMF6_RHIET
Original site: A0A0A8GMF6_RHIET 
ID   A0A0A8GMF6_RHIET        Unreviewed;       377 AA.
AC   A0A0A8GMF6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-SEP-2017, entry version 19.
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=dadX {ECO:0000313|EMBL:AJC83033.1};
GN   ORFNames=IE4803_PC00487 {ECO:0000313|EMBL:AJC83033.1};
OS   Rhizobium etli bv. phaseoli str. IE4803.
OG   Plasmid pRetIE4803c {ECO:0000313|EMBL:AJC83033.1,
OG   ECO:0000313|Proteomes:UP000031160}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=1432049 {ECO:0000313|EMBL:AJC83033.1, ECO:0000313|Proteomes:UP000031160};
RN   [1] {ECO:0000313|EMBL:AJC83033.1, ECO:0000313|Proteomes:UP000031160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IE4803 {ECO:0000313|EMBL:AJC83033.1,
RC   ECO:0000313|Proteomes:UP000031160};
RC   PLASMID=Plasmid pRetIE4803c {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; CP007644; AJC83033.1; -; Genomic_DNA.
DR   RefSeq; WP_040112373.1; NZ_CP007644.1.
DR   EnsemblBacteria; AJC83033; AJC83033; IE4803_PC00487.
DR   KEGG; rep:IE4803_PC00487; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000031160; Plasmid pRetIE4803c.
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; 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:AJC83033.1};
KW   Plasmid {ECO:0000313|EMBL:AJC83033.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      251    377       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    272    272       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     150    150       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     320    320       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   377 AA;  39978 MW;  2D4925F7B403131D CRC64;
     MDSDILVSRA RTATITQGAT GYLTIDLAAL GRNYSKLASM LAPVRAGAVV KADAYGLGAE
     RVAQTLYDQG CRHFFVAQFV EAVRLRPALA EGAQIFVLNG LQPGNELACA ESGIIPVLNS
     LAQWRQWSAT ARRLKRSLPA VLQFDTGMSR LGFPWEERAE LAAAIRDGVN VEILFIMSHL
     ACADELESSQ NGEQIAEMAR IADEFPGFDI SFANSGGVFL GDAYHGVLAR PGIALYGGAP
     NAGGNNPMEP VVRLDVAVVQ TRTVPSGAKI GYGGAHVTRR QTRLATIAAG YADGLPRSLG
     DRGAVYHKGI RLPIVGRVSM DSTTVDITAL PEGALSLGSL VEVLGPNQTL DDVAGDAGTI
     SYEILTGLGD RYDRQYC
//
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