ALR2_ECOL6
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 03-AUG-2022, entry version 114.
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; DOI=10.1128/iai.66.9.4411-4417.1998;
RA Guyer D.M., Kao J.-S., Mobley H.L.T.;
RT "Genomic analysis of a pathogenicity island in uropathogenic Escherichia
RT coli CFT073: distribution of homologous sequences among isolates from
RT patients with pyelonephritis, cystitis, and catheter-associated bacteriuria
RT 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., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT 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 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; AF081283; AAC61705.1; -; Genomic_DNA.
DR EMBL; AE014075; AAN80104.1; -; Genomic_DNA.
DR RefSeq; WP_000197877.1; NC_004431.1.
DR AlphaFoldDB; P59237; -.
DR SMR; P59237; -.
DR STRING; 199310.c1639; -.
DR EnsemblBacteria; AAN80104; AAN80104; c1639.
DR KEGG; ecc:c1639; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_0_6; -.
DR OMA; HMTHFSD; -.
DR BioCyc; ECOL199310:C1639-MON; -.
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 Isomerase; Pyridoxal phosphate.
FT CHAIN 1..356
FT /note="Alanine racemase, catabolic"
FT /id="PRO_0000114518"
FT ACT_SITE 35
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000250"
FT ACT_SITE 253
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 26..27
FT /note="PY -> TH (in Ref. 1; AAC61705)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="L -> I (in Ref. 1; AAC61705)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..172
FT /note="SA -> GR (in Ref. 1; AAC61705)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> S (in Ref. 1; AAC61705)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="Q -> P (in Ref. 1; AAC61705)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="A -> R (in Ref. 1; AAC61705)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="P -> L (in Ref. 1; AAC61705)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="L -> R (in Ref. 1; AAC61705)"
FT /evidence="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
