UXUA_ECOLI
ID UXUA_ECOLI Reviewed; 394 AA.
AC P24215; O87739; Q2M5Z1;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Mannonate dehydratase;
DE EC=4.2.1.8;
DE AltName: Full=D-mannonate hydro-lyase;
GN Name=uxuA; OrderedLocusNames=b4322, JW4285;
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 (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
RC STRAIN=O2:K1:H+ / MT78;
RX PubMed=9766199; DOI=10.1016/s0923-2508(98)80002-8;
RA Marc D., Arne P., Bree A., Dho-Moulin M.;
RT "Colonization ability and pathogenic properties of a fim- mutant of an
RT avian strain of Escherichia coli.";
RL Res. Microbiol. 149:473-485(1998).
RN [6]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC STRAIN=K12;
RX PubMed=3083215; DOI=10.1007/bf00330526;
RA Blanco C., Ritzenthaler P., Kolb A.;
RT "The regulatory region of the uxuAB operon in Escherichia coli K12.";
RL Mol. Gen. Genet. 202:112-119(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC STRAIN=K12;
RX PubMed=8550444; DOI=10.1128/jb.178.1.61-67.1996;
RA Klemm P., Tong S., Nielsen H., Conway T.;
RT "The gntP gene of Escherichia coli involved in gluconate uptake.";
RL J. Bacteriol. 178:61-67(1996).
RN [8]
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).
CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate.
CC {ECO:0000269|PubMed:3038546}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC Xref=Rhea:RHEA:20097, ChEBI:CHEBI:15377, ChEBI:CHEBI:17767,
CC ChEBI:CHEBI:57990; EC=4.2.1.8; 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: By fructuronate. Its expression is subjected to catabolite
CC repression by glucose.
CC -!- SIMILARITY: Belongs to the mannonate dehydratase family. {ECO:0000305}.
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DR EMBL; D13329; BAA02590.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97218.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77278.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78315.1; -; Genomic_DNA.
DR EMBL; AJ225176; CAA12424.1; -; Genomic_DNA.
DR EMBL; X03411; CAA27147.1; ALT_TERM; Genomic_DNA.
DR EMBL; X91735; CAA62860.1; -; Genomic_DNA.
DR PIR; I57745; I57745.
DR PIR; S56547; S56547.
DR RefSeq; NP_418742.1; NC_000913.3.
DR RefSeq; WP_000438562.1; NZ_SSUV01000012.1.
DR PDB; 4EAC; X-ray; 2.30 A; A/B/C/D=1-394.
DR PDB; 4EAY; X-ray; 2.35 A; A/B/C/D=1-394.
DR PDBsum; 4EAC; -.
DR PDBsum; 4EAY; -.
DR AlphaFoldDB; P24215; -.
DR SMR; P24215; -.
DR BioGRID; 4261003; 15.
DR DIP; DIP-11108N; -.
DR IntAct; P24215; 2.
DR STRING; 511145.b4322; -.
DR jPOST; P24215; -.
DR PaxDb; P24215; -.
DR PRIDE; P24215; -.
DR EnsemblBacteria; AAC77278; AAC77278; b4322.
DR EnsemblBacteria; BAE78315; BAE78315; BAE78315.
DR GeneID; 947082; -.
DR KEGG; ecj:JW4285; -.
DR KEGG; eco:b4322; -.
DR PATRIC; fig|1411691.4.peg.2370; -.
DR EchoBASE; EB1059; -.
DR eggNOG; COG1312; Bacteria.
DR HOGENOM; CLU_058621_2_0_6; -.
DR InParanoid; P24215; -.
DR OMA; GIVWALH; -.
DR PhylomeDB; P24215; -.
DR BioCyc; EcoCyc:MANNONDEHYDRAT-MON; -.
DR BioCyc; MetaCyc:MANNONDEHYDRAT-MON; -.
DR BRENDA; 4.2.1.8; 2026.
DR UniPathway; UPA00246; -.
DR PRO; PR:P24215; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc.
DR GO; GO:0008927; F:mannonate dehydratase activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0042840; P:D-glucuronate catabolic process; IMP:EcoCyc.
DR HAMAP; MF_00106; UxuA; 1.
DR InterPro; IPR004628; Man_deHydtase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR PANTHER; PTHR30387; PTHR30387; 1.
DR Pfam; PF03786; UxuA; 1.
DR PIRSF; PIRSF016049; Man_dehyd; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR00695; uxuA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Iron; Lyase; Manganese; Reference proteome.
FT CHAIN 1..394
FT /note="Mannonate dehydratase"
FT /id="PRO_0000170670"
FT VARIANT 52
FT /note="I -> V (in strain: MT78)"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 78..94
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:4EAC"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 205..226
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4EAC"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 323..339
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:4EAC"
FT HELIX 371..391
FT /evidence="ECO:0007829|PDB:4EAC"
SQ SEQUENCE 394 AA; 44838 MW; 0716A50BD6436679 CRC64;
MEQTWRWYGP NDPVSLADVR QAGATGVVTA LHHIPNGEVW SVEEILKRKA IIEDAGLVWS
VVESVPIHED IKTHTGNYEQ WIANYQQTLR NLAQCGIRTV CYNFMPVLDW TRTDLEYVLP
DGSKALRFDQ IEFAAFEMHI LKRPGAEADY TEEEIAQAAE RFATMSDEDK ARLTRNIIAG
LPGAEEGYTL DQFRKHLELY KDIDKAKLRE NFAVFLKAII PVAEEVGVRM AVHPDDPPRP
ILGLPRIVST IEDMQWMVDT VNSMANGFTM CTGSYGVRAD NDLVDMIKQF GPRIYFTHLR
STMREDNPKT FHEAAHLNGD VDMYEVVKAI VEEEHRRKAE GKEDLIPMRP DHGHQMLDDL
KKKTNPGYSA IGRLKGLAEV RGVELAIQRA FFSR
