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   24-JAN-2024, entry version 167.
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; Pseudomonadota; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 511145-b4322; -.
DR   EnsemblBacteria; AAC77278; AAC77278; b4322.
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; ANHLEGD; -.
DR   OrthoDB; 9780250at2; -.
DR   PhylomeDB; P24215; -.
DR   BioCyc; EcoCyc:MANNONDEHYDRAT-MONOMER; -.
DR   BioCyc; MetaCyc:MANNONDEHYDRAT-MONOMER; -.
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:0042840; P:D-glucuronate catabolic process; IMP:EcoCyc.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 2.
DR   HAMAP; MF_00106; UxuA; 1.
DR   InterPro; IPR004628; Man_deHydtase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   NCBIfam; TIGR00695; uxuA; 1.
DR   PANTHER; PTHR30387; MANNONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR30387:SF2; MANNONATE DEHYDRATASE; 1.
DR   Pfam; PF03786; UxuA; 1.
DR   PIRSF; PIRSF016049; Man_dehyd; 1.
DR   SUPFAM; SSF51658; Xylose isomerase-like; 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
//