ID   UXUA_SALPA              Reviewed;         394 AA.
AC   Q5PMP2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   10-JUN-2026, entry version 92.
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=SPA3003;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00106};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-
CC         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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000026; AAV78840.1; -; Genomic_DNA.
DR   RefSeq; WP_000815491.1; NC_006511.1.
DR   AlphaFoldDB; Q5PMP2; -.
DR   SMR; Q5PMP2; -.
DR   KEGG; spt:SPA3003; -.
DR   HOGENOM; CLU_058621_2_0_6; -.
DR   UniPathway; UPA00246; -.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:TreeGrafter.
DR   GO; GO:0030145; F:manganese ion binding; IEA:TreeGrafter.
DR   GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042840; P:D-glucuronate catabolic process; IEA:TreeGrafter.
DR   FunFam; 3.20.20.150:FF:000004; Mannonate dehydratase; 1.
DR   FunFam; 3.20.20.150:FF:000005; Mannonate dehydratase; 1.
DR   Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 2.
DR   HAMAP; MF_00106; UxuA; 1.
DR   InterPro; IPR004628; Man_deHydtase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   NCBIfam; NF003027; PRK03906.1; 1.
DR   NCBIfam; TIGR00695; uxuA; 1.
DR   PANTHER; PTHR30387; MANNONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR30387:SF2; MANNONATE DEHYDRATASE; 1.
DR   Pfam; PF03786; UxuA; 1.
DR   PIRSF; PIRSF016049; Man_dehyd; 1.
DR   SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE   3: Inferred from homology;
KW   Iron; Lyase; Manganese.
FT   CHAIN           1..394
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_0000231055"
SQ   SEQUENCE   394 AA;  44951 MW;  41D3719A0E488E34 CRC64;
     MKQTWRWYGP NDPVTLSDVR QAGATGVVTA LHHIPNGEIW SVDEIQKRKA IVEEAGLEWS
     VVESVPIHED IKTHTGQYDL WIKNYQQTLR NLAQCGIYTV CYNFMPVLDW TRTDLEYVLP
     DGSKALRFDQ IEFAAFELHI LKRPGAEADY TAEEIAQAER RFATMSEEDK ARLTRNIIAG
     LPGAEEGYTL EQFRQHLATY KDIDKAKLRE HFAYFLKAII PVADEVGVRM AVHPDDPPRP
     ILGLPRIVST IEDMQWMVET VNSMANGFTM CTGSYGVRAD NDLVDMIKQF GPRIYFTHLR
     STLREENPKT FHEAAHLHGD VDMYEVVKAI VEEEHRRKAE GSDDLIPMRP DHGHQMLDDL
     KKKTNPGYSA IGRLKGLAEV RGVELAIQRA FFSK
//