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Database: UniProt
Entry: P59237
LinkDB: P59237
Original site: P59237 
ID   ALR2_ECOL6              Reviewed;         356 AA.
AC   P59237;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JAN-2003, sequence version 1.
DT   05-DEC-2018, entry version 105.
DE   RecName: Full=Alanine racemase, catabolic;
DE            EC=5.1.1.1;
GN   Name=dadX; OrderedLocusNames=c1639;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=9712795;
RA   Guyer D.M., Kao J.-S., Mobley H.L.T.;
RT   "Genomic analysis of a pathogenicity island in uropathogenic
RT   Escherichia coli CFT073: distribution of homologous sequences among
RT   isolates from patients with pyelonephritis, cystitis, and catheter-
RT   associated bacteriuria and from fecal samples.";
RL   Infect. Immun. 66:4411-4417(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized
CC       to 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}.
DR   EMBL; AF081283; AAC61705.1; -; Genomic_DNA.
DR   EMBL; AE014075; AAN80104.1; -; Genomic_DNA.
DR   RefSeq; WP_000197877.1; NC_004431.1.
DR   ProteinModelPortal; P59237; -.
DR   SMR; P59237; -.
DR   STRING; 199310.c1639; -.
DR   EnsemblBacteria; AAN80104; AAN80104; c1639.
DR   KEGG; ecc:c1639; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   BioCyc; ECOL199310:C1639-MONOMER; -.
DR   Proteomes; UP000001410; Chromosome.
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   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    356       Alanine racemase, catabolic.
FT                                /FTId=PRO_0000114518.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     130    130       Substrate. {ECO:0000250}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   CONFLICT     26     27       PY -> TH (in Ref. 1; AAC61705).
FT                                {ECO:0000305}.
FT   CONFLICT     50     50       L -> I (in Ref. 1; AAC61705).
FT                                {ECO:0000305}.
FT   CONFLICT    171    172       SA -> GR (in Ref. 1; AAC61705).
FT                                {ECO:0000305}.
FT   CONFLICT    190    190       A -> S (in Ref. 1; AAC61705).
FT                                {ECO:0000305}.
FT   CONFLICT    199    199       Q -> P (in Ref. 1; AAC61705).
FT                                {ECO:0000305}.
FT   CONFLICT    215    215       A -> R (in Ref. 1; AAC61705).
FT                                {ECO:0000305}.
FT   CONFLICT    281    281       P -> L (in Ref. 1; AAC61705).
FT                                {ECO:0000305}.
FT   CONFLICT    292    292       L -> R (in Ref. 1; AAC61705).
FT                                {ECO:0000305}.
SQ   SEQUENCE   356 AA;  38869 MW;  4DF10C5843374659 CRC64;
     MTRPIQASLD LQALKQNLSI VRQAAPYARV WSVVKANAYG HGIERIWSAL GATDGFALLN
     LEEAITLRER GWKGPILMLE GFFHAQDLEI YDQHRLTTCV HSNWQLKALQ NARLKAPLDI
     YLKVNSGMNR LGFQPDRVLT VWQQLRAMAN VGEMTLMSHF AEAEHPDGIS SAMARIEQAA
     EGLECRRSLA NSAATLWHQE AHFDWVRPGI ILYGASPSGQ WRDIANTGLR PVMTLSSEII
     GVQTLKAGER VGYGGRYTAR DEQRIGIVAA GYADGYPRHA PTGTPVLVDG VLTMTVGTVS
     MDMLAVDLTP CPQAGIGTPV ELWGKEIKID DVAAAAGTVG YELMCALALR VPVVTV
//
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