ID   UXUA_SHIF8              Reviewed;         394 AA.
AC   Q0SXM7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   04-NOV-2026, entry version 101.
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=SFV_4204;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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}.
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DR   EMBL; CP000266; ABF06188.1; -; Genomic_DNA.
DR   RefSeq; WP_000438582.1; NC_008258.1.
DR   AlphaFoldDB; Q0SXM7; -.
DR   SMR; Q0SXM7; -.
DR   GeneID; 67174092; -.
DR   GeneID; 93777517; -.
DR   KEGG; sfv:SFV_4204; -.
DR   HOGENOM; CLU_058621_2_0_6; -.
DR   OMA; AACMNAY; -.
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_1000034337"
SQ   SEQUENCE   394 AA;  44824 MW;  49CCE5DB9599B735 CRC64;
     MEQTWRWYGP NDPVSLADVR QAGATGVVTA LHHIPNGEVW SVEEILKRKA IVEDAGLVWS
     VVESVPIHED IKTHTGNYEQ WIANYQQTLR NLAQCGIRTV CYNFMPVLDW TRTDLEYVLP
     DGSKALRFDQ IEFAAFEMHI LKRPGAEADY TEEEIAQAAE RFATMSDEDK ARLTRNIIAG
     LPGAEEGYTL DQFRKHLELY KDIDKAKLRE NFAVFLKAII PVAEEVGVRM AVHPDDPPRP
     ILGLPRIVST IEDMQWMVDT VNSMANGFTM CTGSYGVRAD NDLVDMIKQF GPRIYFTHLR
     STMREDNPKT FHEAAHLNGD VDMYEVVKAI VEEEHRRKAE GKEDLIPMRP DHGHQMLDDL
     KKKTNPGYSA IGRLKGLAEV RGVELAIQRA FFSR
//