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Database: UniProt/SWISS-PROT
Entry: ALR1_AGRFC
LinkDB: ALR1_AGRFC
Original site: ALR1_AGRFC 
ID   ALR1_AGRFC              Reviewed;         391 AA.
AC   P58736;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   07-JUN-2017, entry version 106.
DE   RecName: Full=Alanine racemase, biosynthetic;
DE            EC=5.1.1.1;
GN   Name=alr; OrderedLocusNames=Atu1080; ORFNames=AGR_C_1996;
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: Catalyzes the interconversion of L-alanine and D-
CC       alanine. Provides the D-alanine required for cell wall
CC       biosynthesis (By similarity). {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   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
DR   EMBL; AE007869; AAK86889.1; -; Genomic_DNA.
DR   PIR; AG2709; AG2709.
DR   PIR; H97491; H97491.
DR   RefSeq; NP_354104.1; NC_003062.2.
DR   RefSeq; WP_010971382.1; NC_003062.2.
DR   ProteinModelPortal; P58736; -.
DR   SMR; P58736; -.
DR   STRING; 176299.Atu1080; -.
DR   EnsemblBacteria; AAK86889; AAK86889; Atu1080.
DR   GeneID; 1133118; -.
DR   KEGG; atu:Atu1080; -.
DR   PATRIC; fig|176299.10.peg.1095; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; DTGFNRL; -.
DR   BioCyc; AGRO:ATU1080-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000813; Chromosome circular.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    391       Alanine racemase, biosynthetic.
FT                                /FTId=PRO_0000114492.
FT   ACT_SITE     52     52       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    271    271       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     149    149       Substrate. {ECO:0000250}.
FT   BINDING     330    330       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      52     52       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   391 AA;  42091 MW;  82F6B0320F92B770 CRC64;
     MTDDFEDSFP DNETDAFEQA PLRLTVDLGA LADNWRDMKK RSGRARTAAV VKADAYGLGI
     EDCGATLYHA GARDFFVATV AEGATLRSYA PEARIFVLSG IWQGQERQVF DNDLVPVLAS
     EEQLSFWMAT VAERGDHPCA LHVDTGFNRL GLPLDDALFL ADDVTRPASF DPVLVLSHLA
     CADTPSSPMN RAQLESFRRV SAAFEGIESS LSASAGIFLG PDYHFDLTRP GIALYGGEAV
     NDVANPMRPV AKAEARIIQI REAGEGQTVS YGSSFLLKRA SRLAIASVGY ADGYQRSLSG
     SGIPLREMGH GGAYGVVNGH KVPVAGRVTM DLTIFDVTDV PANAIRAGDY IELFGPNVPV
     DETARAAGTI GYEMLTGLGL RYERQYLVAD D
//
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