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Database: UniProt/TrEMBL
Entry: E3I2D7_RHOVT
LinkDB: E3I2D7_RHOVT
Original site: E3I2D7_RHOVT 
ID   E3I2D7_RHOVT            Unreviewed;       384 AA.
AC   E3I2D7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   07-JUN-2017, entry version 53.
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=Rvan_0945 {ECO:0000313|EMBL:ADP70221.1};
OS   Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 /
OS   LMG 4299).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Hyphomicrobiaceae; Rhodomicrobium.
OX   NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP70221.1, ECO:0000313|Proteomes:UP000001399};
RN   [1] {ECO:0000313|Proteomes:UP000001399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC   {ECO:0000313|Proteomes:UP000001399};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse
RT   alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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; CP002292; ADP70221.1; -; Genomic_DNA.
DR   RefSeq; WP_013418625.1; NC_014664.1.
DR   ProteinModelPortal; E3I2D7; -.
DR   STRING; 648757.Rvan_0945; -.
DR   EnsemblBacteria; ADP70221; ADP70221; Rvan_0945.
DR   KEGG; rva:Rvan_0945; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; RVAN648757:GHZT-946-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001399; 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:UP000001399};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ADP70221.1};
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:UP000001399}.
FT   DOMAIN      251    382       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     52     52       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     325    325       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      52     52       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   384 AA;  41772 MW;  421D2C1868280A01 CRC64;
     MDTGFSEAVE RALAAAPASA NGVLVIRLPA LRRNYRRAAE ASLKAETAAV VKANAYGLGI
     QPVLTALQKE TARTFFVATL DEALALRTFA NDATIYTLNG LMPGTSAVYR DARLRPVLNS
     LAEVEEWSAY CREHEARLPA AIQFDTGMCR VGLEPEAADA LAEKPELLQP FRPAVLMSHL
     VRADEPMHPL NEVQFKRFEA VTSLFPGIAK SLVNSAGCLL RRKYHLDLAR PGIAIYGGNP
     QKVEPSQFEP VVWLFGRIVQ VRHGEKGFTV GYGGTETLRR DSRIATVGVG YADGYFRGVS
     SSDAKPGAVG HIGEHALPLI GRVSMDLTTF DATDVPEALV HRGGFVELLG EKTTVDDLAR
     HAGTIGYEVL TSLGRRYHRV YVDE
//
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