ID   UXUA_YERPG              Reviewed;         397 AA.
AC   A9R4P9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=YpAngola_A1509;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(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; CP000901; ABX86652.1; -; Genomic_DNA.
DR   RefSeq; WP_002208813.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R4P9; -.
DR   SMR; A9R4P9; -.
DR   GeneID; 57977416; -.
DR   KEGG; ypg:YpAngola_A1509; -.
DR   PATRIC; fig|349746.12.peg.2474; -.
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..397
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_1000094230"
SQ   SEQUENCE   397 AA;  44890 MW;  44AA710EED7C2544 CRC64;
     MEQTWRWYGP NDPVSLDDIR QAGATGVVTA LHHIPNGVVW PVSEIKQRQA ELAAKNLVWS
     VVESVPIHED IKTHSGNYQQ YIENYQQTLR NIAECGIDTV CYNFMPILDW TRTDLEYELP
     DGSKALRFDQ IAFAAFELHI LKRPGASNDY TAEEQVQAEA YFNAMTEADI AKLTGNIIAG
     LPGAEEGYTL DQFRARLAEY DGIDKAQLRE NMAYFLRAII PVAEQVGLRM AVHPDDPPRP
     ILGLPRIVST IEDMQWLKET VDSIHNGFTM CTGSYGVRAD NDLVKMIETF GDRIHFTHLR
     STCREGNPKT FHEGGHLQGD VDMYSVVKAI LTEEQRRQSL GDMRPIPMRP DHGHQMLDDL
     HKKTNPGYSA IGRLKGLAEV RGVELALKRT FFPELKQ