ID   UXUA_VIBPA              Reviewed;         395 AA.
AC   Q87FH9;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=VPA1700;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000032; BAC63043.1; -; Genomic_DNA.
DR   RefSeq; NP_801210.1; NC_004605.1.
DR   RefSeq; WP_005477427.1; NC_004605.1.
DR   AlphaFoldDB; Q87FH9; -.
DR   SMR; Q87FH9; -.
DR   STRING; 223926.28810102; -.
DR   EnsemblBacteria; BAC63043; BAC63043; BAC63043.
DR   GeneID; 1192396; -.
DR   KEGG; vpa:VPA1700; -.
DR   PATRIC; fig|223926.6.peg.4616; -.
DR   eggNOG; COG1312; Bacteria.
DR   HOGENOM; CLU_058621_2_0_6; -.
DR   OMA; GIVWALH; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000002493; Chromosome 2.
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; Reference proteome.
FT   CHAIN           1..395
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_0000170691"
SQ   SEQUENCE   395 AA;  44985 MW;  4C978D2E9B15B549 CRC64;
     MEQTWRWYGP NDPVSLDDIR QAGATGIVNA LHHIPNGEVW SKEEILKRKA IIEEKGLTWS
     VVESVPVHEE IKTLTGNFQQ WIDNYKQTLR NLAECGVDTV CYNFMPVLDW TRTDLEFEMP
     DGSKALRFDQ IAFAAFELHI LKRPGAEADY TEAEQAQALE YFNNMTADQI QQLTSNIIAG
     LPGAEEGYTL EEFQAQLDRY AGISKDKLRE HMAYFLSQLM PVCEAHGLKL AVHPDDPPRP
     ILGLPRIVST IEDIDWLTEK VPSKMNGLTM CTGSYGVRGD NDLVKMIKKH GERIYFTHLR
     STKREESNPM TFHEAAHLDG DVDMYNVVMA ILDEEQRRAE VGDHRLIPMR PDHGHQMLDD
     LKKKTNPGYS AIGRLKGLAE VRGLEMALKR AFYTK