ID   KDUI_ECOL5              Reviewed;         278 AA.
AC   Q0TDY9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
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};
GN   OrderedLocusNames=ECP_2856;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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; Evidence={ECO:0000255|HAMAP-
CC         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   -!- SUBUNIT: Homohexamer. {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; CP000247; ABG70840.1; -; Genomic_DNA.
DR   RefSeq; WP_000383248.1; NC_008253.1.
DR   AlphaFoldDB; Q0TDY9; -.
DR   SMR; Q0TDY9; -.
DR   GeneID; 75172927; -.
DR   KEGG; ecp:ECP_2856; -.
DR   HOGENOM; CLU_062609_0_0_6; -.
DR   UniPathway; UPA00545; UER00826.
DR   Proteomes; UP000009182; 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   CDD; cd20491; cupin_KduI_C; 1.
DR   CDD; cd20294; cupin_KduI_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 2.60.120.520; pectin degrading enzyme 5-keto 4- deoxyuronate isomerase, domain 1; 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; 4-DEOXY-L-THREO-5-HEXOSULOSE-URONATE KETOL-ISOMERASE; 1.
DR   PANTHER; PTHR38461:SF1; 4-DEOXY-L-THREO-5-HEXOSULOSE-URONATE KETOL-ISOMERASE; 1.
DR   Pfam; PF04962; KduI; 1.
DR   PIRSF; PIRSF006625; KduI; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 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_1000045082"
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;  31076 MW;  7AF3DD98DE74D597 CRC64;
     MDVRQSIHSA HAKTLDTQGL RNEFLVEKVF VADEYTMVYS HIDRIIVGGI MPVTKTVSVG
     GEVGKQLGVS YFLERRELGV INIGGAGTIT VDGQCYEIGH RDALYVGKGA KEVVFASIDT
     ATPAKFYYNC APAHTTYPTK KVTPDEVSPV TLGDNLTSNR RTINKYFVPD VLETCQLSMG
     LTELAPGNLW NTMPCHTHER RMEVYFYFNM DDDACVFHMM GQPQETRHIV MHNEQAVISP
     SWSIHSGVGT KAYTFIWGMV GENQVFDDMD HVAVKDLR
//