Summary: KduI/IolB family
This is the Wikipedia entry entitled "KduI/IolB isomerase family". More...
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KduI/IolB isomerase family Edit Wikipedia article
|This article is an orphan, as no other articles link to it. (January 2013)|
|crystal structure of 4-deoxy-1-threo-5-hexosulose-uronate ketol-isomerase from enterococcus faecalis|
The family includes 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase (5-keto 4-deoxyuronate isomerase) (KduI) and 5-deoxy-glucuronate isomerase (5DG isomerase) (IolB).
KduI is involved in pectin degradation by free-living soil bacteria that use pectin as a carbon source, breaking it down to 2-keto-3-deoxygluconate, which can ultimately be converted to pyruvate. KduI catalyses the fourth step in pectin degradation, namely the interconversion of 5-keto-4-deoxyuronate and 2,5-diketo-3-dexoygluconate. KduI has a TIM-barrel fold.
This family also includes several bacterial Myo-inositol catabolism proteins, such as IolB, which is encoded by the inositol operon (iolABCDEFGHIJ) in Bacillus subtilis. IolB is involved in myo-inositol catabolism. Glucose repression of the iol operon induced by inositol is exerted through catabolite repression mediated by CcpA and the iol induction system mediated by IolR. Members of this family possess a Cupin like structure.
- Condemine G, Robert-Baudouy J (September 1991). "Analysis of an Erwinia chrysanthemi gene cluster involved in pectin degradation". Mol. Microbiol. 5 (9): 2191–202. PMID 1766386.
- Crowther RL, Georgiadis MM (November 2005). "The crystal structure of 5-keto-4-deoxyuronate isomerase from Escherichia coli". Proteins 61 (3): 680–4. doi:10.1002/prot.20598. PMID 16152643.
- Miwa Y, Fujita Y (October 2001). "Involvement of two distinct catabolite-responsive elements in catabolite repression of the Bacillus subtilis myo-inositol (iol) operon". J. Bacteriol. 183 (20): 5877–84. doi:10.1128/JB.183.20.5877-5884.2001. PMC 99665. PMID 11566986. //www.ncbi.nlm.nih.gov/pmc/articles/PMC99665/.
KduI/IolB family Provide feedback
This family includes the 5-keto 4-deoxyuronate isomerase enzyme EC:184.108.40.206 that is involved in pectin degradation. This family aldo includes bacterial Myo-inositol catabolism (IolB) proteins. The Bacillus subtilis inositol operon (iolABCDEFGHIJ) is involved in myo-inositol catabolism. Glucose repression of the iol operon induced by inositol is exerted through catabolite repression mediated by CcpA and the iol induction system mediated by IolR . The exact function of IolB is unknown. Members of this family possess a Cupin like structure.
Miwa Y, Fujita Y; , J Bacteriol 2001;183:5877-5884.: Involvement of two distinct catabolite-responsive elements in catabolite repression of the Bacillus subtilis myo-inositol (iol) operon. PUBMED:11566986 EPMC:11566986
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR021120
The KduI/IolB family of enzymes includes 5-keto 4-deoxyuronate isomerase (KduI) and 5-deoxy-glucuronate isomerase (IolB).
KduI is involved in pectin degradation by free-living soil bacteria that use pectin as a carbon source, breaking it down to 2-keto-3-deoxygluconate, which can ultimately be converted to pyruvate. KduI catalyses the fourth step in pectin degradation, namely the interconversion of 5-keto-4-deoxyuronate and 2,5-diketo-3-dexoygluconate [PUBMED:1766386]. KduI has a TIM-barrel fold [PUBMED:16152643].
IolB is one of several bacterial proteins encoded by the inositol operon (iolABCDEFGHIJ) in Bacillus subtilis that are involved in myo-inositol catabolism. The enzyme is responsible for isomerization of 5-deoxy-D-glucuronic acid by IolB to produce 2-deoxy-5-keto-D-gluconic acid [PUBMED:18310071]. IolBs possess a cupin-like structure.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||intramolecular oxidoreductase activity, interconverting aldoses and ketoses (GO:0016861)|
|Biological process||metabolic process (GO:0008152)|
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Curation and family details
|Seed source:||COG3717 & Pfam-B_11840 (release 10.0)|
|Number in seed:||72|
|Number in full:||2006|
|Average length of the domain:||252.20 aa|
|Average identity of full alignment:||30 %|
|Average coverage of the sequence by the domain:||91.15 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the KduI domain has been found. There are 16 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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