UXUA_STRU0
ID UXUA_STRU0 Reviewed; 348 AA.
AC B9DSL8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=SUB1202;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR42638.1; -; Genomic_DNA.
DR RefSeq; WP_012658682.1; NC_012004.1.
DR AlphaFoldDB; B9DSL8; -.
DR SMR; B9DSL8; -.
DR STRING; 218495.SUB1202; -.
DR PRIDE; B9DSL8; -.
DR EnsemblBacteria; CAR42638; CAR42638; SUB1202.
DR KEGG; sub:SUB1202; -.
DR eggNOG; COG1312; Bacteria.
DR HOGENOM; CLU_058621_1_0_9; -.
DR OMA; AIVKAYH; -.
DR OrthoDB; 907794at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000000449; 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; Reference proteome.
FT CHAIN 1..348
FT /note="Mannonate dehydratase"
FT /id="PRO_1000197935"
SQ SEQUENCE 348 AA; 39442 MW; 7B8E0522EEACB627 CRC64;
MEMSFRWYGE DDPVTLENIR QIPTMKGIVT AIYDVPVGEV WPRERIQQLK ETVEASGLKI
SVIESVPVHE DIKLGRPTRD VLIDNYIQTI KNLAAEGIDT ICYNFMPVFD WTRTDLAYEY
PDGSTALIFD EEVSKKMDPV NGELSLPGWD SSYTKEEMRA IMDAYADVDE EKLWEHLEYF
IKRIIPEAEA VGVKMAIHPD DPPYSIFGLP RIITGLDSVE RFVNLYDSKS NGITLCVGSY
ASDPKNDVLE ISRRAFELNR VNFVHARNIK LGEGKSFKES AHPSEYGSID MYEVIKLCHE
FGFEGAIRPD HGRMIWGETG RPGYGLYDRA LGATYLSGLY EAVVKAAK