ID   UXUA_ECOSM              Reviewed;         394 AA.
AC   B1LDQ8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Mannonate dehydratase {ECO:0000255|HAMAP-Rule:MF_00106};
DE            EC=4.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00106};
DE   AltName: Full=D-mannonate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00106};
GN   Name=uxuA {ECO:0000255|HAMAP-Rule:MF_00106};
GN   OrderedLocusNames=EcSMS35_4849;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- FUNCTION: Catalyzes the dehydration of D-mannonate. {ECO:0000255|HAMAP-
CC       Rule:MF_00106}.
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:0000255|HAMAP-
CC         Rule:MF_00106};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00106};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00106};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion. {ECO:0000255|HAMAP-Rule:MF_00106}.
CC   -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00106}.
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DR   EMBL; CP000970; ACB19205.1; -; Genomic_DNA.
DR   RefSeq; WP_000438582.1; NC_010498.1.
DR   AlphaFoldDB; B1LDQ8; -.
DR   SMR; B1LDQ8; -.
DR   EnsemblBacteria; ACB19205; ACB19205; EcSMS35_4849.
DR   GeneID; 67416006; -.
DR   KEGG; ecm:EcSMS35_4849; -.
DR   HOGENOM; CLU_058621_2_0_6; -.
DR   OMA; GIVWALH; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000007011; Chromosome.
DR   GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Iron; Lyase; Manganese.
FT   CHAIN           1..394
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_1000197925"
SQ   SEQUENCE   394 AA;  44824 MW;  49CCE5DB9599B735 CRC64;
     MEQTWRWYGP NDPVSLADVR QAGATGVVTA LHHIPNGEVW SVEEILKRKA IVEDAGLVWS
     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