ID   UXUA_STRA3              Reviewed;         348 AA.
AC   Q8E6A2;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=gbs0675;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(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; AL766846; CAD46319.1; -; Genomic_DNA.
DR   RefSeq; WP_000426044.1; NC_004368.1.
DR   AlphaFoldDB; Q8E6A2; -.
DR   SMR; Q8E6A2; -.
DR   STRING; 211110.gbs0675; -.
DR   EnsemblBacteria; CAD46319; CAD46319; CAD46319.
DR   KEGG; san:gbs0675; -.
DR   eggNOG; COG1312; Bacteria.
DR   HOGENOM; CLU_058621_1_0_9; -.
DR   OMA; AIVKAYH; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000823; 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..348
FT                   /note="Mannonate dehydratase"
FT                   /id="PRO_0000170687"
SQ   SEQUENCE   348 AA;  39263 MW;  2D135E69A7C9C4DA CRC64;
     MEMSFRWYGE DDPVTLENIG QIPTMKGIVT AIYDVPVGEV WSRERIQQLK EKVEAAGLKI
     SVIESVPVHE DIKLGRPTRD LLIDNYIQTV KNLAAEGIDT ICYNFMPVFD WTRTDLAYQY
     PDGSTALIFD ETVSKKMDPV NGELSLPGWD ASYSKEEMKA IMDAYAEIDE EKLWENLTYF
     IKRIIPEAEA VGVKMAIHPD DPPYSIFGLP RIITGLEAIE RFVKLYDSKS NGITLCVGSY
     ASDPQNDVLE ISRRAFELDR VNFVHARNIK LGDGKSFKES AHPSEYGSID MYEVIKLCHE
     FGFEGAIRPD HGRMIWGETG RPGYGLYDRA LGATYLSGLY EAVIKGSK