ID   UXUA_HISS2              Reviewed;         394 AA.
AC   B0URI0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   18-JUN-2025, entry version 81.
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=HSM_0415;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000947; ACA32058.1; -; Genomic_DNA.
DR   RefSeq; WP_012341261.1; NC_010519.1.
DR   AlphaFoldDB; B0URI0; -.
DR   SMR; B0URI0; -.
DR   STRING; 228400.HSM_0415; -.
DR   GeneID; 31486695; -.
DR   KEGG; hsm:HSM_0415; -.
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; 1.
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_1000075901"
SQ   SEQUENCE   394 AA;  44914 MW;  71A85CC165ED9D48 CRC64;
     MEQTWRWYGP NDPVSLDDVR QAGATGVVTA LHHIPNGQVW SVEEINKRKA LLEEKGLVWS
     VVESVPIHED IKTQTGNYQQ WIDNYKQTLR NLASCGIDIV CYNFMPVLDW TRTDLEYEMP
     DGSKALRFDQ VAFAAFELYI LKRPGAEETY SPEEQAEAKA YFDQMSEADI AKLTKNIIAG
     LPGSEEGYTL EEFQAQLDRY KGISTEKFRT HLAYFLNEIV PVAQEVGIRM AIHPDDPPRP
     ILGLPRIVST IDDMQWFVDT QPLAANGFTF CTGSYGVLAE NDLVKMAEKF ADRIYFVHLR
     STQREENPRS FHEADHLAGD VNMFGVTKAL LTEEYRRKAN GDNRLIPMRP DHGHQMLDDL
     KKKTNPGYSA IGRLRGLAEF RGLELALKKV YFND
//