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KDUI_YERE8
ID   KDUI_YERE8              Reviewed;         278 AA.
AC   A1JMF5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
DE            EC=5.3.1.17 {ECO:0000255|HAMAP-Rule:MF_00687};
DE   AltName: Full=5-keto-4-deoxyuronate isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
DE   AltName: Full=DKI isomerase {ECO:0000255|HAMAP-Rule:MF_00687};
GN   Name=kduI {ECO:0000255|HAMAP-Rule:MF_00687}; OrderedLocusNames=YE1888;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-
CC       glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate.
CC       {ECO:0000255|HAMAP-Rule:MF_00687}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D-glycero-2,5-
CC         hexodiulosonate; Xref=Rhea:RHEA:23896, ChEBI:CHEBI:17117,
CC         ChEBI:CHEBI:29071; EC=5.3.1.17; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00687};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00687};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00687};
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00687}.
CC   -!- SIMILARITY: Belongs to the KduI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00687}.
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DR   EMBL; AM286415; CAL11967.1; -; Genomic_DNA.
DR   RefSeq; WP_011816214.1; NC_008800.1.
DR   RefSeq; YP_001006149.1; NC_008800.1.
DR   AlphaFoldDB; A1JMF5; -.
DR   SMR; A1JMF5; -.
DR   STRING; 393305.YE1888; -.
DR   PRIDE; A1JMF5; -.
DR   EnsemblBacteria; CAL11967; CAL11967; YE1888.
DR   KEGG; yen:YE1888; -.
DR   PATRIC; fig|393305.7.peg.2042; -.
DR   eggNOG; COG3717; Bacteria.
DR   HOGENOM; CLU_062609_0_0_6; -.
DR   OMA; TFIWAMA; -.
DR   UniPathway; UPA00545; UER00826.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0008697; F:4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.10; -; 1.
DR   Gene3D; 2.60.120.520; -; 1.
DR   HAMAP; MF_00687; KduI; 1.
DR   InterPro; IPR007045; KduI.
DR   InterPro; IPR021120; KduI/IolB_isomerase.
DR   InterPro; IPR027449; KduI_N.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR38461; PTHR38461; 1.
DR   Pfam; PF04962; KduI; 1.
DR   PIRSF; PIRSF006625; KduI; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Isomerase; Metal-binding; Zinc.
FT   CHAIN           1..278
FT                   /note="4-deoxy-L-threo-5-hexosulose-uronate ketol-
FT                   isomerase"
FT                   /id="PRO_1000045095"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
FT   BINDING         245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00687"
SQ   SEQUENCE   278 AA;  31190 MW;  669565C4F85BB62D CRC64;
     MQICQSIHSD HARQLDTAGL RREFLIENIF VSDEYTMTYS HIDRIIVGGI LPVEKTVSIG
     DEVGKQLGVS YFLERRELGV INIGGPGLIT VDGQVYEIGN QEALYVGKGA KEVTFNSLES
     SKPAKFYYNS APAHTTYPNK KITLAEAAPQ TLGDDATSNR RTINKYIVPD VLPTCQLTMG
     LTKLAPGNLW NTMPCHTHDR RMEVYFYFDM DEETAVFHMM GQAQETRHLL VHNEQAVISP
     SWSIHSGVGT KRYTFIWGMV GENQVFGDMD HIAVSELR
 
 
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