|Gene:||kduI||Accession Numbers: G7463 (EcoCyc), b2843, ECK2841|
Subunit composition of
5-dehydro-4-deoxy-D-glucuronate isomerase = [KduI]6
predicted 5-keto 4-deoxyuronate isomerase monomer = KduI
KduI was a predicted 5-keto 4-deoxyuronate isomerase due to its high sequence similarity to the enzyme from Erwinia chrysanthemi. In unpurified form, the enzyme appeares to be able to utilize both glucuronate and galacturonate, perhaps catalyzing the same reaction as UxaC. While UxaC expression is repressed under osmotic stress conditions, KduI expression appears to be unaffected, and it could therefore substitute for UxaC [Rothe13]. The purified protein was recently shown to catalyze the activity of EC 184.108.40.206, 5-dehydro-4-deoxy-D-glucuronate isomerase in coupled assays with KduD from Pectobacterium carotovorum or Streptococcus agalactiae [Maruyama15].
Crystal structures of KduI have been solved [Dunten98, Crowther05]. The enzyme binds a metal ion tentatively identified as Zn2+ and is structurally similar to members of the cupin superfamily of proteins [Crowther05]. In vivo homomultimeric KduI interaction can be detected in cross-linking experiments [Zheng11].
KduI was identified as a protein whose expression is 8-fold lower in E. coli found in the cecum of mice that were fed a casein diet compared to mice fed a starch diet [Rothe12]. Expression of kduI is increased in the presence of galacturonate and glucuronate [Rothe13].
|Map Position: [2,981,310 <- 2,982,146] (64.26 centisomes, 231°)||Length: 837 bp / 278 aa|
Molecular Weight of Polypeptide: 31.076 kD (from nucleotide sequence), 33.0 kD (experimental) [Dunten98]
Molecular Weight of Multimer: 165.0 kD (experimental) [Crowther05]
Unification Links: ASAP:ABE-0009332, DIP:DIP-10069N, EchoBASE:EB2899, EcoGene:EG13096, EcoliWiki:b2843, ModBase:Q46938, OU-Microarray:b2843, PortEco:kduI, PR:PRO_000023059, Pride:Q46938, Protein Model Portal:Q46938, RefSeq:NP_417320, RegulonDB:G7463, SMR:Q46938, String:511145.b2843, Swiss-Model:Q46938, UniProt:Q46938
Relationship Links: InterPro:IN-FAMILY:IPR007045, InterPro:IN-FAMILY:IPR011051, InterPro:IN-FAMILY:IPR021120, InterPro:IN-FAMILY:IPR027447, InterPro:IN-FAMILY:IPR027449, Panther:IN-FAMILY:PTHR30025:SF0, PDB:Structure:1X8M, PDB:Structure:1XRU, Pfam:IN-FAMILY:PF04962
|MultiFun Terms:||metabolism → carbon utilization → carbon compounds|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB Lennox||Yes||37||Aerobic||7||Yes [Baba06, Comment 1]|
|M9 medium with 1% glycerol||Yes||37||Aerobic||7.2||0.35||Yes [Joyce06, Comment 2]|
|MOPS medium with 0.4% glucose||Yes||37||Aerobic||7.2||0.22||Yes [Baba06, Comment 1]|
Enzymatic reaction of: 5-dehydro-4-deoxy-D-glucuronate isomerase
EC Number: 220.127.116.11-dehydro-4-deoxy-D-glucuronate ⇄ 3-deoxy-D-glycero-2,5-hexodiulosonate
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction of enzyme catalysis.
This reaction is reversible.
|Pfam PF04962||31 -> 273|
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.
Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371
Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394
Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726
Maruyama15: Maruyama Y, Oiki S, Takase R, Mikami B, Murata K, Hashimoto W (2015). "Metabolic Fate of Unsaturated Glucuronic/Iduronic Acids from Glycosaminoglycans: Molecular identification and structure determination of streptococcal isomerase and dehydrogenase." J Biol Chem 290(10);6281-92. PMID: 25605731
Rodina11: Rodina E, Vorobieva N, Kurilova S, Mikulovich J, Vainonen J, Aro EM, Nazarova T (2011). "Identification of new protein complexes of Escherichia coli inorganic pyrophosphatase using pull-down assay." Biochimie 93(9);1576-83. PMID: 21664227
Rothe12: Rothe M, Alpert C, Engst W, Musiol S, Loh G, Blaut M (2012). "Impact of nutritional factors on the proteome of intestinal Escherichia coli: induction of OxyR-dependent proteins AhpF and Dps by a lactose-rich diet." Appl Environ Microbiol 78(10);3580-91. PMID: 22427493
Rothe13: Rothe M, Alpert C, Loh G, Blaut M (2013). "Novel Insights into E. coli's Hexuronate Metabolism: KduI Facilitates the Conversion of Galacturonate and Glucuronate under Osmotic Stress Conditions." PLoS One 8(2);e56906. PMID: 23437267
Zheng11: Zheng C, Yang L, Hoopmann MR, Eng JK, Tang X, Weisbrod CR, Bruce JE (2011). "Cross-linking measurements of in vivo protein complex topologies." Mol Cell Proteomics 10(10);M110.006841. PMID: 21697552
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493