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Database: UniProt/TrEMBL
Entry: L0LYG2_RHITR
LinkDB: L0LYG2_RHITR
Original site: L0LYG2_RHITR 
ID   L0LYG2_RHITR            Unreviewed;       363 AA.
AC   L0LYG2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   28-MAR-2018, 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=alr2 {ECO:0000313|EMBL:AGB75184.1};
GN   ORFNames=RTCIAT899_PC06965 {ECO:0000313|EMBL:AGB75184.1};
OS   Rhizobium tropici CIAT 899.
OG   Plasmid pRtrCIAT899c {ECO:0000313|EMBL:AGB75184.1,
OG   ECO:0000313|Proteomes:UP000010996}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=698761 {ECO:0000313|EMBL:AGB75184.1, ECO:0000313|Proteomes:UP000010996};
RN   [1] {ECO:0000313|EMBL:AGB75184.1, ECO:0000313|Proteomes:UP000010996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 899 {ECO:0000313|EMBL:AGB75184.1,
RC   ECO:0000313|Proteomes:UP000010996};
RC   PLASMID=Plasmid pRtrCIAT899c {ECO:0000313|Proteomes:UP000010996};
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}.
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; CP004018; AGB75184.1; -; Genomic_DNA.
DR   ProteinModelPortal; L0LYG2; -.
DR   EnsemblBacteria; AGB75184; AGB75184; RTCIAT899_PC06965.
DR   KEGG; rtr:RTCIAT899_PC06965; -.
DR   PATRIC; fig|698761.4.peg.6047; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000010996; Plasmid pRtrCIAT899c.
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:UP000010996};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Plasmid {ECO:0000313|EMBL:AGB75184.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010996}.
FT   DOMAIN      237    363       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    258    258       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     306    306       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   363 AA;  38568 MW;  92CEA3213A598A27 CRC64;
     MDSGACGYLT VDLAALSRNY DKLSAIVAPA KTAAVVKADS YGLGANQVSK TLYGRGCRHF
     FVAHFIEALR LRPQLAGDAA IFVLNGLLPG NEATCADGGI VPVINSLDQL QQWSQTARSL
     QRRLPAVLQF DTGMSRLGIP PEDRGVVATH LQTSDDIDIL FIMSHLASAD EVGNEQNADQ
     LAEMRRVAAE FPQYDVSFAN SGGIFLGGDF HGVLARPGIA LYGGAPTGGV ANPMEAVVRL
     DVAVVQTRTV LEGARVGYGG VHVTKGRTRL ATIAAGYADG LPRSLSDRGA VYYNGVRLPI
     VGRVSMDSAT IDISALPEGA LSFGSMVEVL GDHQTVDDLA RDAGLISYEI LTSLGHRFHR
     QYR
//
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