Summary: PEP-utilising enzyme, mobile domain
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PEP-utilising enzyme, mobile domain Provide feedback
This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it.
Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, Noh SJ, Dunaway-Mariano D; , Proc Natl Acad Sci U S A 1996;93:2652-2657.: Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites. PUBMED:8610096 EPMC:8610096
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008279A number of enzymes that catalyze the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) via a phospho-histidine intermediate have been shown to be structurally related [PUBMED:7686067, PUBMED:8973315, PUBMED:2176881, PUBMED:1557039]. All these enzymes share the same catalytic mechanism: they bind PEP and transfer the phosphoryl group from it to a histidine residue. This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it [PUBMED:12083528]. It is often found associated with the pyruvate phosphate dikinase, PEP/pyruvate-binding domain (INTERPRO) at its N terminus.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||transferase activity, transferring phosphorus-containing groups (GO:0016772)|
|Biological process||phosphorylation (GO:0016310)|
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Curation and family details
|Author:||Finn RD, Griffiths-Jones SR|
|Number in seed:||179|
|Number in full:||11592|
|Average length of the domain:||81.70 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||11.56 %|
|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:||18|
|Download:||download the raw HMM for this family|
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There are 7 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 PEP-utilizers domain has been found. There are 47 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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