ID KDUI_ECOLI Reviewed; 278 AA. AC Q46938; Q2M9Z4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-DEC-2013, entry version 105. DE RecName: Full=4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase; DE EC=5.3.1.17; DE AltName: Full=5-keto-4-deoxyuronate isomerase; DE AltName: Full=DKI isomerase; GN Name=kduI; Synonyms=yqeE; OrderedLocusNames=b2843, JW2811; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [3] RP PROTEIN SEQUENCE OF 1-20 AND 227-247, CRYSTALLIZATION, AND SUBUNIT. RX PubMed=9761873; DOI=10.1107/S090744499701785X; RA Dunten P., Jaffe H., Aksamit R.R.; RT "Crystallization of 5-keto-4-deoxyuronate isomerase from Escherichia RT coli."; RL Acta Crystallogr. D 54:678-680(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 1-276 IN COMPLEX WITH ZINC, RP COFACTOR, AND SUBUNIT. RC STRAIN=K12 / DH5-alpha; RX PubMed=16152643; DOI=10.1002/prot.20598; RA Crowther R.L., Georgiadis M.M.; RT "The crystal structure of 5-keto-4-deoxyuronate isomerase from RT Escherichia coli."; RL Proteins 61:680-684(2005). CC -!- FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D- CC glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate (By CC similarity). CC -!- CATALYTIC ACTIVITY: 5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D- CC glycero-2,5-hexodiulosonate. CC -!- COFACTOR: Binds 1 zinc ion per subunit (Probable). The bound metal CC seen in the crystal structure was tentatively identified as zinc, CC and its requirement for activity has not been shown. CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy- CC D-gluconate from pectin: step 4/5. CC -!- SUBUNIT: Homohexamer. CC -!- SIMILARITY: Belongs to the KduI family. 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; U29581; AAB40490.1; -; Genomic_DNA. DR EMBL; U00096; AAC75882.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76912.1; -; Genomic_DNA. DR PIR; D65067; D65067. DR RefSeq; NP_417320.1; NC_000913.2. DR RefSeq; YP_491048.1; NC_007779.1. DR PDB; 1X8M; X-ray; 2.60 A; A/B/C/D/E/F=2-278. DR PDB; 1XRU; X-ray; 1.94 A; A/B=1-276. DR PDBsum; 1X8M; -. DR PDBsum; 1XRU; -. DR ProteinModelPortal; Q46938; -. DR SMR; Q46938; 1-277. DR DIP; DIP-10069N; -. DR IntAct; Q46938; 2. DR STRING; 511145.b2843; -. DR PaxDb; Q46938; -. DR PRIDE; Q46938; -. DR DNASU; 947319; -. DR EnsemblBacteria; AAC75882; AAC75882; b2843. DR EnsemblBacteria; BAE76912; BAE76912; BAE76912. DR GeneID; 12932950; -. DR GeneID; 947319; -. DR KEGG; ecj:Y75_p2777; -. DR KEGG; eco:b2843; -. DR PATRIC; 32121104; VBIEscCol129921_2941. DR EchoBASE; EB2899; -. DR EcoGene; EG13096; kduI. DR eggNOG; COG3717; -. DR HOGENOM; HOG000124379; -. DR KO; K01815; -. DR OMA; IWAMAGE; -. DR OrthoDB; EOG664CJZ; -. DR ProtClustDB; PRK00924; -. DR BioCyc; EcoCyc:G7463-MONOMER; -. DR BioCyc; ECOL316407:JW2811-MONOMER; -. DR BioCyc; MetaCyc:G7463-MONOMER; -. DR BRENDA; 5.3.1.17; 2026. DR UniPathway; UPA00545; UER00826. DR EvolutionaryTrace; Q46938; -. DR PRO; PR:Q46938; -. DR Genevestigator; Q46938; -. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0008697; F:4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019698; P:D-galacturonate catabolic process; IDA:EcoCyc. DR GO; GO:0042840; P:D-glucuronate catabolic process; IDA:EcoCyc. DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.60.120.500; -; 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; IPR027447; KduI_C. DR InterPro; IPR027449; KduI_N. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF04962; KduI; 1. DR PIRSF; PIRSF006625; KduI; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; Isomerase; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1 278 4-deoxy-L-threo-5-hexosulose-uronate FT ketol-isomerase. FT /FTId=PRO_0000215485. FT METAL 196 196 Zinc. FT METAL 198 198 Zinc. FT METAL 203 203 Zinc. FT METAL 245 245 Zinc. FT STRAND 2 4 FT HELIX 9 12 FT HELIX 17 24 FT STRAND 38 40 FT TURN 41 44 FT STRAND 45 51 FT STRAND 53 55 FT STRAND 57 60 FT HELIX 61 66 FT STRAND 69 71 FT TURN 72 75 FT STRAND 76 82 FT STRAND 87 91 FT STRAND 94 98 FT STRAND 103 106 FT STRAND 113 118 FT STRAND 126 132 FT STRAND 140 142 FT HELIX 144 147 FT STRAND 150 152 FT HELIX 155 157 FT STRAND 161 168 FT TURN 169 171 FT STRAND 178 184 FT STRAND 190 192 FT STRAND 194 197 FT STRAND 201 209 FT STRAND 216 222 FT STRAND 225 231 FT STRAND 233 239 FT STRAND 244 251 FT STRAND 254 262 FT STRAND 269 272 FT HELIX 274 277 SQ SEQUENCE 278 AA; 31076 MW; F7CD5C259503CD1A CRC64; MDVRQSIHSA HAKTLDTQGL RNEFLVEKVF VADEYTMVYS HIDRIIVGGI MPITKTVSVG GEVGKQLGVS YFLERRELGV INIGGAGTIT VDGQCYEIGH RDALYVGKGA KEVVFASIDT GTPAKFYYNC APAHTTYPTK KVTPDEVSPV TLGDNLTSNR RTINKYFVPD VLETCQLSMG LTELAPGNLW NTMPCHTHER RMEVYFYFNM DDDACVFHMM GQPQETRHIV MHNEQAVISP SWSIHSGVGT KAYTFIWGMV GENQVFDDMD HVAVKDLR //