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 07-NOV-2018, entry version 135. 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; Enterobacterales; 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 277:1453-1462(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 INDUCTION. RC STRAIN=K12; RX PubMed=22427493; DOI=10.1128/AEM.00244-12; RA Rothe M., Alpert C., Engst W., Musiol S., Loh G., Blaut M.; RT "Impact of nutritional factors on the proteome of intestinal RT Escherichia coli: induction of OxyR-dependent proteins AhpF and Dps by RT a lactose-rich diet."; RL Appl. Environ. Microbiol. 78:3580-3591(2012). RN [5] RP FUNCTION, AND INDUCTION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=23437267; DOI=10.1371/journal.pone.0056906; RA Rothe M., Alpert C., Loh G., Blaut M.; RT "Novel insights into E. coli's hexuronate metabolism: KduI facilitates RT the conversion of galacturonate and glucuronate under osmotic stress RT conditions."; RL PLoS ONE 8:E56906-E56906(2013). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS). RA Fedorov A.A., Fedorov E.V., Almo S.C.; RT "The crystal structure of pectin degrading enzyme 5-keto 4- RT deoxyuronate isomerase from Escherichia coli."; RL Submitted (AUG-2004) to the PDB data bank. RN [7] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, RP 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). Plays a role in the catabolism of hexuronates under CC osmotic stress conditions, likely substituting for the regular CC hexuronate degrading enzyme UxaC whose expression is repressed in CC these conditions (PubMed:23437267). {ECO:0000250|UniProtKB:Q05529, CC ECO:0000269|PubMed:23437267}. CC -!- CATALYTIC ACTIVITY: 5-dehydro-4-deoxy-D-glucuronate = 3-deoxy-D- CC glycero-2,5-hexodiulosonate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:16152643, ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. The bound metal seen in the CC crystal structure was tentatively identified as zinc, and its CC requirement for activity has not been shown. CC {ECO:0000269|PubMed:16152643, ECO:0000305}; CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy- CC D-gluconate from pectin: step 4/5. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:16152643, CC ECO:0000269|PubMed:9761873}. CC -!- INDUCTION: Its expression is up-regulated in the presence of CC galacturonate and glucuronate (PubMed:23437267). Is also down- CC regulated in E.coli of mice fed a casein-rich diet CC (PubMed:22427493). {ECO:0000269|PubMed:22427493, CC ECO:0000269|PubMed:23437267}. CC -!- SIMILARITY: Belongs to the KduI family. {ECO:0000305}. 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_000913.3. DR RefSeq; WP_000383237.1; NZ_LN832404.1. 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=1-278. DR PDBsum; 1X8M; -. DR PDBsum; 1XRU; -. DR ProteinModelPortal; Q46938; -. DR SMR; Q46938; -. DR BioGrid; 4261944; 15. DR DIP; DIP-10069N; -. DR IntAct; Q46938; 2. DR STRING; 316385.ECDH10B_3015; -. DR PaxDb; Q46938; -. DR PRIDE; Q46938; -. DR DNASU; 947319; -. DR EnsemblBacteria; AAC75882; AAC75882; b2843. DR EnsemblBacteria; BAE76912; BAE76912; BAE76912. DR GeneID; 947319; -. DR KEGG; ecj:JW2811; -. DR KEGG; eco:b2843; -. DR PATRIC; fig|1411691.4.peg.3891; -. DR EchoBASE; EB2899; -. DR EcoGene; EG13096; kduI. DR eggNOG; ENOG4105D50; Bacteria. DR eggNOG; COG3717; LUCA. DR HOGENOM; HOG000124379; -. DR InParanoid; Q46938; -. DR KO; K01815; -. DR PhylomeDB; Q46938; -. DR BioCyc; EcoCyc:G7463-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 Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; HDA:UniProtKB. DR GO; GO:0008697; F:4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase activity; IDA:EcoCyc. 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-UniRule. 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-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 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. {ECO:0000269|PubMed:16152643}. FT METAL 198 198 Zinc. {ECO:0000269|PubMed:16152643}. FT METAL 203 203 Zinc. {ECO:0000269|PubMed:16152643}. FT METAL 245 245 Zinc. {ECO:0000269|PubMed:16152643}. FT STRAND 2 4 {ECO:0000244|PDB:1XRU}. FT HELIX 9 12 {ECO:0000244|PDB:1XRU}. FT HELIX 17 24 {ECO:0000244|PDB:1XRU}. FT STRAND 38 40 {ECO:0000244|PDB:1XRU}. FT TURN 41 44 {ECO:0000244|PDB:1XRU}. FT STRAND 45 51 {ECO:0000244|PDB:1XRU}. FT STRAND 53 55 {ECO:0000244|PDB:1XRU}. FT STRAND 57 60 {ECO:0000244|PDB:1XRU}. FT HELIX 61 66 {ECO:0000244|PDB:1XRU}. FT STRAND 69 71 {ECO:0000244|PDB:1XRU}. FT TURN 72 75 {ECO:0000244|PDB:1XRU}. FT STRAND 76 82 {ECO:0000244|PDB:1XRU}. FT STRAND 87 91 {ECO:0000244|PDB:1XRU}. FT STRAND 94 98 {ECO:0000244|PDB:1XRU}. FT STRAND 103 106 {ECO:0000244|PDB:1XRU}. FT STRAND 113 118 {ECO:0000244|PDB:1XRU}. FT STRAND 126 132 {ECO:0000244|PDB:1XRU}. FT STRAND 140 142 {ECO:0000244|PDB:1XRU}. FT HELIX 144 147 {ECO:0000244|PDB:1XRU}. FT STRAND 150 152 {ECO:0000244|PDB:1XRU}. FT HELIX 155 157 {ECO:0000244|PDB:1XRU}. FT STRAND 161 168 {ECO:0000244|PDB:1XRU}. FT TURN 169 171 {ECO:0000244|PDB:1XRU}. FT STRAND 178 184 {ECO:0000244|PDB:1XRU}. FT STRAND 190 192 {ECO:0000244|PDB:1XRU}. FT STRAND 194 197 {ECO:0000244|PDB:1XRU}. FT STRAND 201 209 {ECO:0000244|PDB:1XRU}. FT STRAND 216 222 {ECO:0000244|PDB:1XRU}. FT STRAND 225 231 {ECO:0000244|PDB:1XRU}. FT STRAND 233 239 {ECO:0000244|PDB:1XRU}. FT STRAND 244 251 {ECO:0000244|PDB:1XRU}. FT STRAND 254 262 {ECO:0000244|PDB:1XRU}. FT STRAND 269 272 {ECO:0000244|PDB:1XRU}. FT HELIX 274 277 {ECO:0000244|PDB:1XRU}. 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 //