Summary: Phosphoribosyl transferase domain
Phosphoribosyl transferase domain Provide feedback
This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:220.127.116.11, P07672. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase P51900. Hypoxanthine phosphoribosyl-transferase EC:18.104.22.168 P36766. Ribose-phosphate pyrophosphokinase i EC:22.214.171.124 P09329. Amidophosphoribosyltransferase EC:126.96.36.199 P00496. Orotate phosphoribosyl-transferase EC:188.8.131.52 P11172. Uracil phosphoribosyl-transferase EC:184.108.40.206 P25532. Xanthine-guanine phosphoribosyl-transferase EC:220.127.116.11 P00501. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain .
Islam MR, Kim H, Kang SW, Kim JS, Jeong YM, Hwang HJ, Lee SY, Woo JC, Kim SG;, Plant Mol Biol. 2007;63:465-477.: Functional characterization of a gene encoding a dual domain for uridine kinase and uracil phosphoribosyltransferase in Arabidopsis thaliana. PUBMED:17143579 EPMC:17143579
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000836
The name PRT comes from phosphoribosyltransferase (PRTase) enzymes, which carry out phosphoryl transfer reactions on 5-phosphoribosyl-alpha1-pyrophosphate PRPP, an activated form of ribose-5-phosphate. Members of Phosphoribosyltransferase (PRT) are catalytic and are regulatory proteins involved in nucleotide synthesis and salvage [PUBMED:11751055]. This includes a range of diverse phosphoribosyl transferase enzymes including adenine phosphoribosyltransferase (EC); hypoxanthine-guanine-xanthine phosphoribosyltransferase; hypoxanthine phosphoribosyltransferase (EC); ribose-phosphate pyrophosphokinase (EC); amidophosphoribosyltransferase (EC); orotate phosphoribosyltransferase (EC);uracil phosphoribosyltransferase (EC); and xanthine-guanine phosphoribosyltransferase (EC).
Not all PRT proteins are enzymes. For example, in some bacteria PRT proteins regulate the expression of purine and pyrimidine synthetic genes.
Members of PRT are defined by the protein fold and by a short 13-residue sequence motif, The motif consists of four hydrophobic amino acids, two acidic amino acids and seven amino acids of variable character, usually including glycine and threonine. The motif has been predicted to be a PRPP-binding site in advance of structural information [PUBMED:3009477, PUBMED:3527873]. Apart of this motif, different PRT proteins have a low level of sequence identity, less than 15%. The PRT sequence motif is only found in PRTases from the nucleotide synthesis and salvage pathways. Other PRTases, from the tryptophan, histidine and nicotinamide synthetic and salvage pathways, lack the PRT sequence motif and appear to be unrelated to each other and unrelated to the PRT family.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||nucleoside metabolic process (GO:0009116)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This superfamily of phosphoribosyl-transferases (PRTases) and phosphoribosyl-pyrophosphate synthetase-like protein families is characterised by a core fold of three layers, a/b/a with a mixed beta-sheet of six strands. In one of the families consists of two domains of this fold.
The clan contains the following 6 members:Pribosyl_synth Pribosyltran PRTase_1 PRTase_2 PRTase_3 UPRTase
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Bateman A|
|Author:||Bateman A, Sonnhammer ELL, Finn RD|
|Number in seed:||71|
|Number in full:||30853|
|Average length of the domain:||121.40 aa|
|Average identity of full alignment:||18 %|
|Average coverage of the sequence by the domain:||48.82 %|
|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:||22|
|Download:||download the raw HMM for this family|
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There are 3 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 Pribosyltran domain has been found. There are 299 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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