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Database: UniProt/SWISS-PROT
Entry: ALR2_AGRFC
LinkDB: ALR2_AGRFC
Original site: ALR2_AGRFC 
ID   ALR2_AGRFC              Reviewed;         388 AA.
AC   P58737;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   23-MAY-2018, entry version 103.
DE   RecName: Full=Alanine racemase, catabolic;
DE            EC=5.1.1.1;
GN   Name=dadB; OrderedLocusNames=Atu3292; ORFNames=AGR_L_3051;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium
OS   tumefaciens (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P.,
RA   Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L.,
RA   Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr.,
RA   Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C.,
RA   Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A.,
RA   Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D.,
RA   Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M.,
RA   Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M.,
RA   Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V.,
RA   Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
RA   Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
RA   Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
RA   Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
RA   Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
RA   Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized
CC       to pyruvate by DadA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
DR   EMBL; AE007870; AAK90098.1; -; Genomic_DNA.
DR   PIR; AF2961; AF2961.
DR   PIR; H98321; H98321.
DR   RefSeq; NP_357313.1; NC_003063.2.
DR   RefSeq; WP_010972917.1; NC_003063.2.
DR   ProteinModelPortal; P58737; -.
DR   SMR; P58737; -.
DR   STRING; 176299.Atu3292; -.
DR   PRIDE; P58737; -.
DR   EnsemblBacteria; AAK90098; AAK90098; Atu3292.
DR   GeneID; 1135166; -.
DR   KEGG; atu:Atu3292; -.
DR   PATRIC; fig|176299.10.peg.3133; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   BioCyc; AGRO:ATU3292-MONOMER; -.
DR   Proteomes; UP000000813; Chromosome linear.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
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; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    388       Alanine racemase, catabolic.
FT                                /FTId=PRO_0000114493.
FT   ACT_SITE     46     46       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     145    145       Substrate. {ECO:0000250}.
FT   BINDING     315    315       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      46     46       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   388 AA;  40616 MW;  5F6A9FCB73CBED1B CRC64;
     MDMQISRQQA AGGASGHLTI DLGALRDNYL TLAGMAPASQ TAAVVKADAY GLGADVVSQT
     LFEAGCRNFF VAHIDEALAL RLRLSAKARI FVLNGLQPGN ETSCAAMAIT PVLNSLEQIA
     QWSAHARELG KTLTAAVQID TGMCRLGLSP EELEILSAKQ QLLDGIEIAF VMSHLACADE
     PDHVSNAAQL AVMRKAATAF PETPVCFSNS GGIFLGNDYH NALLRPGIAL YGGAPSAAGP
     NPMKPVVRLD VAVIQTRTVP AGSLVGYGGS FTASVPTRLA TIAAGYADGL PRSLSNRGAA
     WYNGVRLPIA GRVSMDSIIL DISALPEGTL TQGSLVQMIG PDQTLEDIAE DAGTIAYEIL
     TGLGRRYRRS YIQPGMSPAT ASTSVNHK
//
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