UXUA_ECO7I
ID UXUA_ECO7I Reviewed; 394 AA.
AC B7NV92;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=ECIAI39_4795;
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928164; CAR20892.1; -; Genomic_DNA.
DR RefSeq; WP_000438591.1; NC_011750.1.
DR RefSeq; YP_002410650.1; NC_011750.1.
DR AlphaFoldDB; B7NV92; -.
DR SMR; B7NV92; -.
DR STRING; 585057.ECIAI39_4795; -.
DR EnsemblBacteria; CAR20892; CAR20892; ECIAI39_4795.
DR GeneID; 66671795; -.
DR KEGG; ect:ECIAI39_4795; -.
DR PATRIC; fig|585057.6.peg.4950; -.
DR HOGENOM; CLU_058621_2_0_6; -.
DR OMA; GIVWALH; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000000749; 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_1000197929"
SQ SEQUENCE 394 AA; 44794 MW; 247A3B474C542325 CRC64;
MEQTWRWYGP NDPVSLADVR QAGATGVVTA LHHIPNGEVW SVEEILKRKA IVEDAGLVWS
VVESVPIHED IKTHTGNYEQ WIANYQQTLR NLAQCGIRTV CYNFMPVLDW TRTDLEYVLP
DGSKALRFDQ IEFAAFEMHI LKRPGAEADY TEEEIAQAAV RFATMSDEDK ARLTRNIIAG
LPGAEEGYTL DQFRKHLELY KDIDKAKLRE NFAVFLKAII PVAEEVGVRM AVHPDDPPRP
ILGLPRIVST IEDMQWMVDT VNSMANGFTM CTGSYGVRAD NDLVDMIKQF GPRIYFTHLR
STMREDNPKT FHEAAHLNGD VDMYEVVKAI VEEEHRRKAE GKEDLIPMRP DHGHQMLDDL
KKKTNPGYSA IGRLKGLAEV RGVELAIQRA FFSR