ID   UXUA_BRUSU              Reviewed;         401 AA.
AC   Q8FVM2; G0KDH8;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=BRA0814, BS1330_II0807;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014292; AAN33990.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM20266.1; -; Genomic_DNA.
DR   RefSeq; WP_004690313.1; NZ_KN046805.1.
DR   AlphaFoldDB; Q8FVM2; -.
DR   SMR; Q8FVM2; -.
DR   PRIDE; Q8FVM2; -.
DR   EnsemblBacteria; AEM20266; AEM20266; BS1330_II0807.
DR   GeneID; 45053830; -.
DR   GeneID; 55592464; -.
DR   KEGG; bms:BRA0814; -.
DR   KEGG; bsi:BS1330_II0807; -.
DR   PATRIC; fig|204722.22.peg.2186; -.
DR   HOGENOM; CLU_058621_2_0_5; -.
DR   OMA; AIVKAYH; -.
DR   PhylomeDB; Q8FVM2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000007104; Chromosome II.
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..401
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_0000170667"
SQ   SEQUENCE   401 AA;  44445 MW;  399192F5F46A0921 CRC64;
     MRQAWRWFGP EAGVPLDAVR QAGATDIVSA LHEVPIGQEW TSAQIVERKN LIESTPTGRH
     PLTWSVVESI PVSDDIKRSG KAARHDIGAW IASMEALARN DIKVICYNFM PVVDWCRTDL
     DYITSTGATA MRFDQDRFAA FDLHILQRKG AEKDYSEEDR IAARAIFEAM DETEIEQLIV
     NIASALPGST TEPLTIPAFR EKLETYASID AAHLRRNLVE FLEAVTPVAD SLGVKLTLHP
     DDPPRSLFGL PRIASTEADY AAIFAAVPAQ SNGMCFCTGS LGVRADNDLP AIARRFASRI
     HFSHLRATTR EGDGRTFHEA AHLEGDVDMV GILRILLEED RKRDAGQTII FRSDHGHRMM
     DDLEKKVTPG YPVIGRMRGL AELRGIITAL DACALEYDPN V