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Database: UniProt/TrEMBL
Entry: L0LHB4_RHITR
LinkDB: L0LHB4_RHITR
Original site: L0LHB4_RHITR 
ID   L0LHB4_RHITR            Unreviewed;       387 AA.
AC   L0LHB4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-SEP-2017, entry version 35.
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=alr1 {ECO:0000313|EMBL:AGB70612.1};
GN   ORFNames=RTCIAT899_CH06025 {ECO:0000313|EMBL:AGB70612.1};
OS   Rhizobium tropici CIAT 899.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=698761 {ECO:0000313|EMBL:AGB70612.1, ECO:0000313|Proteomes:UP000010996};
RN   [1] {ECO:0000313|EMBL:AGB70612.1, ECO:0000313|Proteomes:UP000010996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 899 {ECO:0000313|EMBL:AGB70612.1};
RX   PubMed=23270491; DOI=10.1186/1471-2164-13-735;
RA   Ormeno-Orrillo E., Menna P., Almeida L.G., Ollero F.J., Nicolas M.F.,
RA   Pains Rodrigues E., Shigueyoshi Nakatani A., Silva Batista J.S.,
RA   Oliveira Chueire L.M., Souza R.C., Ribeiro Vasconcelos A.T.,
RA   Megias M., Hungria M., Martinez-Romero E.;
RT   "Genomic basis of broad host range and environmental adaptability of
RT   Rhizobium tropici CIAT 899 and Rhizobium sp. PRF 81 which are used in
RT   inoculants for common bean (Phaseolus vulgaris L.).";
RL   BMC Genomics 13:735-735(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; CP004015; AGB70612.1; -; Genomic_DNA.
DR   RefSeq; WP_015339340.1; NC_020059.1.
DR   ProteinModelPortal; L0LHB4; -.
DR   EnsemblBacteria; AGB70612; AGB70612; RTCIAT899_CH06025.
DR   GeneID; 32498039; -.
DR   KEGG; rtr:RTCIAT899_CH06025; -.
DR   PATRIC; fig|698761.4.peg.1254; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000010996; 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; 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:UP000010996};
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      244    381       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     46     46       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    265    265       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     143    143       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     324    324       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      46     46       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   387 AA;  41534 MW;  BD883F6B8F330C45 CRC64;
     MTDNFNDDDA FASAGLRLTV DLGALVENWC DLARRSGKAR TSAVVKADAY GLGIEDVGET
     LYGAGARDFF VATADEGTTL RLYAPEARIF VLSGIWPGME RRFFENDLVP VIASEEQLTF
     WMSVLSDYGD YPCALQVDTG FNRLGLPMGD AIALADDVSR PASFAPVLVM SHLACGDDPA
     NAMNRQQLEA FRKVSTAFEG IEASLANSAG IFLGADYHFD LTRPGIATYG GEAVPGVANP
     MRPVATAEAR IIQTRSVKSG ETVGYGRALQ LTRDSRLAIV SAGYADGYMR SQSSAGVPLR
     QTGIPGGHGF IAGHKVPVAG RITMDLTIFD VTDLPENLVR AGDYVELFGS NISVDEAARA
     AGTIGYEMLT SMGLRHERRY ISEQTEE
//
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