ID KDUI_ECO5E Reviewed; 278 AA. AC B5Z4G1; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 02-DEC-2020, entry version 71. 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=ECH74115_4112; OS Escherichia coli O157:H7 (strain EC4115 / EHEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=444450; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=EC4115 / EHEC; RX PubMed=22135463; DOI=10.1073/pnas.1107176108; RA Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A.; RT "Genomic anatomy of Escherichia coli O157:H7 outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20142-20147(2011). 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 -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00687}. CC -!- SIMILARITY: Belongs to the KduI family. {ECO:0000255|HAMAP- CC Rule:MF_00687}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001164; ACI38163.1; -; Genomic_DNA. DR RefSeq; WP_000383257.1; NC_011353.1. DR SMR; B5Z4G1; -. DR EnsemblBacteria; ACI38163; ACI38163; ECH74115_4112. DR KEGG; ecf:ECH74115_4112; -. DR HOGENOM; CLU_062609_0_0_6; -. DR OMA; TFIWAMA; -. DR UniPathway; UPA00545; UER00826. 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_1000131879" FT METAL 196 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687" FT METAL 198 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687" FT METAL 203 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687" FT METAL 245 FT /note="Zinc" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00687" SQ SEQUENCE 278 AA; 31090 MW; B8E4098A31BEB6A2 CRC64; MDVRQSIHSA HAKTLETQGL RNEFLVEKVF VADEYTMVYS HIDRIIIGGI MPVTKTVSVG GEVGKQLGVS YFLERRELGV INIGGAGTIT VDGQCYEIGH RDALYVGKGA KEVVFASIDT GTPAKFYYNC APAHTTYPTK KVTPDEVSPV TLGDNLTSNR RTINKYFVPD VLETCQLSMG LTELAPGNLW NTMPCHTHER RMEVYFYFNM DDDACVFHMM GQPQETRHIV MHNEQAVISP SWSIHSGVGT KAYTFIWGMV GENQVFDDMD HVAVKDLR //