ID   UXUA_CLOPE              Reviewed;         350 AA.
AC   Q8XP15;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=CPE0151;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB79857.1; -; Genomic_DNA.
DR   RefSeq; WP_011009639.1; NC_003366.1.
DR   AlphaFoldDB; Q8XP15; -.
DR   SMR; Q8XP15; -.
DR   STRING; 195102.gene:10489395; -.
DR   EnsemblBacteria; BAB79857; BAB79857; BAB79857.
DR   KEGG; cpe:CPE0151; -.
DR   HOGENOM; CLU_058621_1_0_9; -.
DR   OMA; AIVKAYH; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000818; 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; 2.
PE   3: Inferred from homology;
KW   Iron; Lyase; Manganese; Reference proteome.
FT   CHAIN           1..350
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_0000170669"
SQ   SEQUENCE   350 AA;  40293 MW;  80FB0F9CFFD78A0B CRC64;
     MEMTFRWYGK DDPVKLEYIK QIPGMKGIVT AIYDIPVGEV WPLERILELK KEIESHGLKL
     SVIESVPVHE DIKLGLPTRD RYIDNYIQTI RNLAEAGVDT ICYNFMPVFD WTRSDLNYKL
     EDGSTCLIYD EEQVKKMDPA LGELELPGWD TSYGEGGLKG LLEQYKDIDE EILWSNLNYF
     IQRIMKVADK VRMKMAIHPD DPPWGIFGLP RIITNFDNLK RFIDLYDSPY HGITLCTGSL
     GCTKVNDMVQ MINYFGKERN RIHFAHLRNV KITGDSSFNE VAHLSEAGSL DFYEIVKAYC
     DYDFAGPYRP DHGRMIWGET GRPGYGLYDR ALGAVYINGL IEAIKKNKKN