UXAA_ECOLI
ID UXAA_ECOLI Reviewed; 495 AA.
AC P42604; Q2M9B5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Altronate dehydratase;
DE EC=4.2.1.7;
DE AltName: Full=D-altronate hydro-lyase;
GN Name=uxaA; Synonyms=ygjW; OrderedLocusNames=b3091, JW3062;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Mizobuchi K.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PH DEPENDENCE, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12;
RX PubMed=3038546; DOI=10.1111/j.1432-1033.1987.tb13559.x;
RA Dreyer J.L.;
RT "The role of iron in the activation of mannonic and altronic acid
RT hydratases, two Fe-requiring hydro-lyases.";
RL Eur. J. Biochem. 166:623-630(1987).
RN [5]
RP OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=19429622; DOI=10.1128/jb.00108-09;
RA Shimada T., Yamamoto K., Ishihama A.;
RT "Involvement of the leucine response transcription factor LeuO in
RT regulation of the genes for sulfa drug efflux.";
RL J. Bacteriol. 191:4562-4571(2009).
CC -!- FUNCTION: Catalyzes the dehydration of D-altronate.
CC {ECO:0000269|PubMed:3038546}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-altronate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC Xref=Rhea:RHEA:15957, ChEBI:CHEBI:15377, ChEBI:CHEBI:17360,
CC ChEBI:CHEBI:57990; EC=4.2.1.7; Evidence={ECO:0000269|PubMed:3038546};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:3038546};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:3038546};
CC Note=Mn(2+) can substitute for iron, but in higher concentrations.
CC Cannot use Fe(3+), Ni(2+) or Mg(2+). {ECO:0000269|PubMed:3038546};
CC -!- ACTIVITY REGULATION: Is inhibited by high concentrations of Fe(2+) (> 2
CC mM), and by EDTA or other iron chelators in vitro.
CC {ECO:0000269|PubMed:3038546}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is about 7.5. The activity at pH 6.5 and 8.6 is only about
CC 20% of the maximal achievable activity at optimum pH.
CC {ECO:0000269|PubMed:3038546};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion.
CC -!- INDUCTION: Repressed by LeuO and H-NS. Part of the uxaCA operon.
CC {ECO:0000269|PubMed:19429622}.
CC -!- SIMILARITY: Belongs to the UxaA family. {ECO:0000305}.
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DR EMBL; D13328; BAA18901.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57893.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76126.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77141.1; -; Genomic_DNA.
DR PIR; H65097; H65097.
DR RefSeq; NP_417562.1; NC_000913.3.
DR RefSeq; WP_001199390.1; NZ_LN832404.1.
DR AlphaFoldDB; P42604; -.
DR SMR; P42604; -.
DR BioGRID; 4262407; 12.
DR DIP; DIP-11105N; -.
DR IntAct; P42604; 6.
DR STRING; 511145.b3091; -.
DR jPOST; P42604; -.
DR PaxDb; P42604; -.
DR PRIDE; P42604; -.
DR EnsemblBacteria; AAC76126; AAC76126; b3091.
DR EnsemblBacteria; BAE77141; BAE77141; BAE77141.
DR GeneID; 947603; -.
DR KEGG; ecj:JW3062; -.
DR KEGG; eco:b3091; -.
DR PATRIC; fig|1411691.4.peg.3638; -.
DR EchoBASE; EB2592; -.
DR eggNOG; COG2721; Bacteria.
DR HOGENOM; CLU_029189_0_0_6; -.
DR InParanoid; P42604; -.
DR OMA; MRHDKRE; -.
DR PhylomeDB; P42604; -.
DR BioCyc; EcoCyc:ALTRODEHYDRAT-MON; -.
DR BioCyc; MetaCyc:ALTRODEHYDRAT-MON; -.
DR UniPathway; UPA00246; -.
DR PRO; PR:P42604; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008789; F:altronate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0019698; P:D-galacturonate catabolic process; IMP:EcoCyc.
DR CDD; cd11613; SAF_AH_GD; 1.
DR InterPro; IPR007392; Gal/Altron_deHydtase_C.
DR InterPro; IPR013974; SAF.
DR InterPro; IPR044144; UxaA/GarD_SAF.
DR Pfam; PF04295; GD_AH_C; 1.
DR Pfam; PF08666; SAF; 1.
DR SMART; SM00858; SAF; 1.
PE 1: Evidence at protein level;
KW Iron; Lyase; Manganese; Reference proteome.
FT CHAIN 1..495
FT /note="Altronate dehydratase"
FT /id="PRO_0000172283"
SQ SEQUENCE 495 AA; 54093 MW; 480B21A93624FF32 CRC64;
MQYIKIHALD NVAVALADLA EGTEVSVDNQ TVTLRQDVAR GHKFALTDIA KGANVIKYGL
PIGYALADIA AGVHVHAHNT RTNLSDLDQY RYQPDFQDLP AQAADREVQI YRRANGDVGV
RNELWILPTV GCVNGIARQI QNRFLKETNN AEGTDGVFLF SHTYGCSQLG DDHINTRTML
QNMVRHPNAG AVLVIGLGCE NNQVAAFRET LGDIDPERVH FMICQQQDDE IEAGIEHLHQ
LYNVMRNDKR EPGKLSELKF GLECGGSDGL SGITANPMLG RFSDYVIANG GTTVLTEVPE
MFGAEQLLMD HCRDEATFEK LVTMVNDFKQ YFIAHDQPIY ENPSPGNKAG GITTLEDKSL
GCTQKAGSSV VVDVLRYGER LKTPGLNLLS APGNDAVATS ALAGAGCHMV LFSTGRGTPY
GGFVPTVKIA TNSELAAKKK HWIDFDAGQL IHGKAMPQLL EEFIDTIVEF ANGKQTCNER
NDFRELAIFK SGVTL
