ID   UXUA_CROS8              Reviewed;         396 AA.
AC   A7MLL8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ESA_01068;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU76336.1; -; Genomic_DNA.
DR   RefSeq; WP_012124262.1; NC_009778.1.
DR   AlphaFoldDB; A7MLL8; -.
DR   SMR; A7MLL8; -.
DR   PRIDE; A7MLL8; -.
DR   EnsemblBacteria; ABU76336; ABU76336; ESA_01068.
DR   KEGG; esa:ESA_01068; -.
DR   PATRIC; fig|290339.8.peg.944; -.
DR   HOGENOM; CLU_058621_2_0_6; -.
DR   OMA; GIVWALH; -.
DR   OrthoDB; 907794at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000260; 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..396
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_1000034327"
SQ   SEQUENCE   396 AA;  44961 MW;  B39F2669DE98DBBB CRC64;
     MEQTWRWYGP NDPVSLDDIR QAGATGIVTA LHHIPNGEVW PVEEIKKRQA ELAQKGLTWS
     VVESIPVHED IKTHTGQYDR YIASYQQSIR NLAACGIDTV CYNFMPILDW TRTDLEYTLP
     DGSKALRFDH IAFAAFELHI LKRDGARHDY TDDEQRQAQD YFSAMSEAQI ETLTRNIIAG
     LPGAEEGYTL DQFRARLSEY DHIDKTALRD NMAYFLKAIV PVAEEAGVRL AVHPDDPPRP
     ILGLPRIVST IEDMQWLKET VDSIHNGFTM CTGSYGVRAD NDLVRMVETF ADRIHFTHLR
     STCREANPKT FHEAAHLYGD VDMVAVVKAI LTEEQRRKKA GDLRPIPFRP DHGHQMLDDL
     RKKTNPGYSA IGRLKGLAEV RGVELALKKV LFPDLL