ID   UXUA_PECCP              Reviewed;         398 AA.
AC   C6DAZ5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-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=PC1_0987;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT12037.1; -; Genomic_DNA.
DR   RefSeq; WP_012773673.1; NC_012917.1.
DR   AlphaFoldDB; C6DAZ5; -.
DR   SMR; C6DAZ5; -.
DR   STRING; 561230.PC1_0987; -.
DR   EnsemblBacteria; ACT12037; ACT12037; PC1_0987.
DR   KEGG; pct:PC1_0987; -.
DR   eggNOG; COG1312; Bacteria.
DR   HOGENOM; CLU_058621_2_0_6; -.
DR   OMA; GIVWALH; -.
DR   OrthoDB; 907794at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000002736; 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..398
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_1000202870"
FT   REGION          342..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  44960 MW;  E42722376B0999C0 CRC64;
     MEQTWRWYGP NDPVSLDDVR QAGATGVVTA LHHIPNGEIW SIEEIEKRKA ELKAKGLVWS
     VVESVPVHEE IKTQTGNYQQ HIANYQQSLR NLAQCGIDTV CYNFMPVLDW TRTDLEYVLP
     DGSKALRFDH IAFAAFELHI LKRHGAENDY TADEQAQAAD YFRAMSEEEI ARLTGNIIAG
     LPGSEEGYTL EQFRSRLAEY DGIDHAKLRE HLGHFLREIV PVAEAAGIRL AIHPDDPPRP
     ILGLPRVMST IDDMRWLKQT VDSLHNGFTF CTGSYGVRAD NDLVTMLETF ADRVHFTHLR
     ATCREDNPNS FHEGAHLQGD VDMVAIINAI LAEELRRQKA GDRRPIPMRP DHGHQMLDDL
     KKKTNPGYSA IGRLKGLAEL RGVELALKRT LFTELQQG