ID   UXUA_BRUME              Reviewed;         401 AA.
AC   Q8YCQ4;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=BMEII0474;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53716.1; -; Genomic_DNA.
DR   PIR; AI3568; AI3568.
DR   RefSeq; WP_004682164.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YCQ4; -.
DR   SMR; Q8YCQ4; -.
DR   STRING; 224914.BMEII0474; -.
DR   EnsemblBacteria; AAL53716; AAL53716; BMEII0474.
DR   GeneID; 29595241; -.
DR   KEGG; bme:BMEII0474; -.
DR   PATRIC; fig|224914.52.peg.2897; -.
DR   eggNOG; COG1312; Bacteria.
DR   OMA; AIVKAYH; -.
DR   PhylomeDB; Q8YCQ4; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000419; 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_0000170666"
SQ   SEQUENCE   401 AA;  44473 MW;  CE8A825653711FE3 CRC64;
     MRQAWRWFGP EAGVPLDAVR QAGATDIVSA LHEVPIGQEW TSAQIVERKN LIESTPTGRH
     PLTWSVVESI PVSDDIKRSG KAARHDIGAW IASMEALARN DIKVICYNFM PVVDWCRTDL
     DYITSTGATA MRFDQDRFAA FDLHILRRKG AEKDYSEEDR IAARAIFEAM DETEIEQLIV
     NIASALPGST TEPLTIPAFR KKLETYASID AAHLRRNLVE FLEAVTPVAD SLGVKLTLHP
     DDPPRSLFGL PRIASTEADY AAIFAAVPAQ SNGMCFCTGS LGVRADNDLP AIARRFASRI
     HFSHLRATTR EGDGRTFHEA AHLEGDVDMV GILRILLEED RKRDAGQTII FRSDHGHRMM
     DDLEKKVTPG YPVIGRMRGL AELRGIITAL DACALEYDPN V