ID   UXUA_THEMA              Reviewed;         360 AA.
AC   Q9WXS4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Mannonate dehydratase;
DE            EC=4.2.1.8;
DE   AltName: Full=D-mannonate hydro-lyase;
GN   Name=uxuA; OrderedLocusNames=TM_0069;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Catalyzes the dehydration of D-mannonate. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC       interconversion.
CC   -!- SIMILARITY: Belongs to the mannonate dehydratase family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD35163.1; -; Genomic_DNA.
DR   PIR; A72423; A72423.
DR   RefSeq; NP_227885.1; NC_000853.1.
DR   RefSeq; WP_004082566.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WXS4; -.
DR   SMR; Q9WXS4; -.
DR   STRING; 243274.THEMA_04460; -.
DR   EnsemblBacteria; AAD35163; AAD35163; TM_0069.
DR   KEGG; tma:TM0069; -.
DR   eggNOG; COG1312; Bacteria.
DR   InParanoid; Q9WXS4; -.
DR   OMA; GIVWALH; -.
DR   OrthoDB; 907794at2; -.
DR   BioCyc; MetaCyc:MON-17955; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR   GO; GO:0008927; F:mannonate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0042840; P:D-glucuronate catabolic process; IBA:GO_Central.
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..360
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_0000170689"
SQ   SEQUENCE   360 AA;  41890 MW;  08C9771F1DCBFA3E CRC64;
     MKLVFRWYGE KHDTVTLEQI RQIPGVEGVV GALFDIPVGE VWPFEEIMKL KETVEKAGLK
     LEVIESVNVH EDIKLGLPTR DRYIENYKKT IRNLAKAGVK VVCYNFMPVF DWMRTDLHKK
     LPDGSETMEY DHRLIEGVTP DELIKRVKEG SQGFVLPGWE WDRLEKLRET FELYKNVDEE
     KLFENLVYFL ERVIPVCEEC DVKLAIHPDD PPWSIFGLPR IITNKENIER MLKAVDSPYN
     GITFCMGSLG ANPENNIPEM IRYFGKMGRI HFAHVRNLKF TGEKSFYETA HPSFCGSHDL
     FEVMKAFHDI GYEGYIRPDH GRLIWGEKAR PGYGLYDRAL GATYILGLWE AIDKMKKRYC