ID   UXUA_ECOBW              Reviewed;         394 AA.
AC   C4ZT10;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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}; OrderedLocusNames=BWG_4020;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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; CP001396; ACR63722.1; -; Genomic_DNA.
DR   RefSeq; WP_000438562.1; NC_012759.1.
DR   AlphaFoldDB; C4ZT10; -.
DR   SMR; C4ZT10; -.
DR   PRIDE; C4ZT10; -.
DR   KEGG; ebw:BWG_4020; -.
DR   HOGENOM; CLU_058621_2_0_6; -.
DR   OMA; GIVWALH; -.
DR   UniPathway; UPA00246; -.
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_1000202868"
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