Summary: Ketopantoate hydroxymethyltransferase
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Ketopantoate hydroxymethyltransferase ( EC:22.214.171.124) is the first enzyme in the pantothenate biosynthesis pathway.
Jones CE, Brook JM, Buck D, Abell C, Smith AG; , J Bacteriol 1993;175:2125-2130.: Cloning and sequencing of the Escherichia coli panB gene, which encodes ketopantoate hydroxymethyltransferase, and overexpression of the enzyme. PUBMED:8096212 EPMC:8096212
Internal database links
|SCOOP:||NanE AroM DUF1961 Peptidase_M76 DUF3663 PEP_mutase Asp_Glu_race_2 UPF0731 DUF4861|
|Similarity to PfamA using HHSearch:||PEP_mutase|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003700
The panB gene from Escherichia coli encodes the first enzyme of the pantothenate biosynthesis pathway, ketopantoate hydroxymethyltransferase (KPHMT) EC. Fungal ketopantoate hydroxymethyltransferase is essential for the biosynthesis of coenzyme A, while the pathway intermediate 4'-phosphopantetheine is required for penicillin production [PUBMED:10503542].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||3-methyl-2-oxobutanoate hydroxymethyltransferase activity (GO:0003864)|
|Biological process||pantothenate biosynthetic process (GO:0015940)|
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This superfamily consists of a number of TIM barrel domains found in enzymes such as pyruvate kinase, malate synthase and citrate lyase.
The clan contains the following 11 members:C-C_Bond_Lyase HpcH_HpaI ICL Malate_synthase Pantoate_transf PEP-utilizers_C PEP_hydrolase PEP_mutase PEPcase PEPcase_2 PK
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Curation and family details
|Author:||Mian N, Bateman A|
|Number in seed:||778|
|Number in full:||16931|
|Average length of the domain:||253.50 aa|
|Average identity of full alignment:||50 %|
|Average coverage of the sequence by the domain:||93.51 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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There is 1 interaction 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 Pantoate_transf domain has been found. There are 45 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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