ID   UXUA_ENDTX              Reviewed;         364 AA.
AC   B1GZ70;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=TGRD_069;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
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; AP009510; BAG13552.1; -; Genomic_DNA.
DR   RefSeq; WP_015423081.1; NC_020419.1.
DR   RefSeq; YP_001956013.1; NC_020419.1.
DR   AlphaFoldDB; B1GZ70; -.
DR   SMR; B1GZ70; -.
DR   STRING; 471821.TGRD_069; -.
DR   EnsemblBacteria; BAG13552; BAG13552; TGRD_069.
DR   KEGG; rsd:TGRD_069; -.
DR   PATRIC; fig|471821.5.peg.110; -.
DR   HOGENOM; CLU_058621_1_0_0; -.
DR   OMA; GIVWALH; -.
DR   OrthoDB; 907794at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000001691; Chromosome.
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..364
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_1000094228"
SQ   SEQUENCE   364 AA;  42121 MW;  539CCD6FFF36EABB CRC64;
     MKMTFRWYGE NVDPIPLRYI RQIPGVEGIV WALHDIPAGE CWTVERIEEV KAQAAKYNFN
     TDVVESVNVH EDIKLGLPSR KKYIENYKNT LKNLGRAGVK VVCYNFMPVF DWTRTDLYKP
     QSDGSTALFY EKAKVDNINP VKFLEQMSKQ EGLLTMPGWE PERLSKIKEL FEAYKEIKDD
     DLWENLKYFL QEIIPVAQES GIKMAIHPDD PPWSIFGLSR IITCRDNIKK FLSLVDNPSN
     GLTLCSGSLG SCTKNNIAAI VREFGDRIYF AHIRNIRHFK NGDFTETSHK TSDGSLDITE
     IVKAYHDINY KYYVRPDHGR HIWDEKCRPG YGLYDRSLGI MYIFGLWDAF EKISASKRGQ
     YGVE