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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   03-AUG-2022, entry version 119.
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 tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
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., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., 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., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., 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 to
CC       pyruvate by DadA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
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}.
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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   AlphaFoldDB; P58737; -.
DR   SMR; P58737; -.
DR   STRING; 176299.Atu3292; -.
DR   EnsemblBacteria; AAK90098; AAK90098; Atu3292.
DR   GeneID; 66223602; -.
DR   KEGG; atu:Atu3292; -.
DR   PATRIC; fig|176299.10.peg.3133; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_1_5; -.
DR   OMA; HMTHFSD; -.
DR   PhylomeDB; P58737; -.
DR   BioCyc; AGRO:ATU3292-MON; -.
DR   Proteomes; UP000000813; Chromosome linear.
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:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
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   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..388
FT                   /note="Alanine racemase, catabolic"
FT                   /id="PRO_0000114493"
FT   ACT_SITE        46
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        267
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         46
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="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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