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50  structures 3887  species 0  interactions 4587  sequences 31  architectures

Family: HisG_C (PF08029)

Summary: HisG, C-terminal domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "ATP phosphoribosyltransferase". More...

ATP phosphoribosyltransferase Edit Wikipedia article

In enzymology, an ATP phosphoribosyltransferase (EC 2.4.2.17) is an enzyme that catalyzes the chemical reaction

1-(5-phospho-D-ribosyl)-ATP + diphosphate ATP + 5-phospho-alpha-D-ribose 1-diphosphate

Thus, the two substrates of this enzyme are 1-(5-phospho-D-ribosyl)-ATP and diphosphate, whereas its two products are ATP and 5-phospho-alpha-D-ribose 1-diphosphate.

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is 1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-alpha-D-ribosyl-transferase. Other names in common use include phosphoribosyl-ATP pyrophosphorylase, adenosine triphosphate phosphoribosyltransferase, phosphoribosyladenosine triphosphate:pyrophosphate, phosphoribosyltransferase, phosphoribosyl ATP synthetase, phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase, phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase, phosphoribosyladenosine triphosphate pyrophosphorylase, and phosphoribosyladenosine triphosphate synthetase. This enzyme participates in histidine metabolism.

Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1H3D, 1NH7, 1NH8, 1O63, 1O64, 1Q1K, 1USY, 1VE4, 1Z7M, and 1Z7N.

References

Template:Enzyme references

  • AMES BN, MARTIN RG, GARRY BJ (1961). "The first step of histidine biosynthesis". J. Biol. Chem. 236: 2019–26. PMID 13682989.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Martin RG (1963). "The phosphorolysis of nucleosides by rabbit bone marrow: The nature of feedback inhibition by histidine". J. Biol. Chem. 238: 257–268.
  • Voll MJ, Appella E, Martin RG (1967). "Purification and composition studies of phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of histidine biosynthesis". J. Biol. Chem. 242: 1760–7. PMID 5337591.{{cite journal}}: CS1 maint: multiple names: authors list (link)

External links

The CAS registry number for this enzyme class is Template:CAS registry.

Template:Enzyme links

Gene Ontology (GO) codes

Template:GO code links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

HisG, C-terminal domain Provide feedback

No Pfam abstract.

This tab holds annotation information from the InterPro database.

InterPro entry IPR013115

ATP phosphoribosyltransferase ( EC ) is the enzyme that catalyzes the first step in the biosynthesis of histidine in bacteria, fungi and plants as shown below. It is a member of the larger phosphoribosyltransferase superfamily of enzymes which catalyse the condensation of 5-phospho-alpha-D-ribose 1-diphosphate with nitrogenous bases in the presence of divalent metal ions [ PUBMED:11751055 ].

ATP + 5-phospho-alpha-D-ribose 1-diphosphate = 1-(5-phospho-D-ribosyl)-ATP + diphosphate

Histidine biosynthesis is an energetically expensive process and ATP phosphoribosyltransferase activity is subject to control at several levels. Transcriptional regulation is based primarily on nutrient conditions and determines the amount of enzyme present in the cell, while feedback inihibition rapidly modulates activity in response to cellular conditions. The enzyme has been shown to be inhibited by 1-(5-phospho-D-ribosyl)-ATP, histidine, ppGpp (a signal associated with adverse environmental conditions) and ADP and AMP (which reflect the overall energy status of the cell). As this pathway of histidine biosynthesis is present only in prokayrotes, plants and fungi, this enzyme is a promising target for the development of novel antimicrobial compounds and herbicides.

This entry represents the C-terminal portion of ATP phosphoribosyltransferase. The enzyme itself exists in equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates [ PUBMED:14741209 , PUBMED:12511575 ]. Interconversion between the various forms is largely reversible and is influenced by the binding of the natural substrates and inhibitors of the enzyme. This domain is not directly involved in catalysis but appears to be responsible for the formation of hexamers induced by the binding of inhibitors to the enzyme, thus regulating activity.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan GlnB-like (CL0089), which has the following description:

The members of this clan are characterised by the fact the domains, each comprised of four beta-strand and two alpha helices, tend to form tetrameric structures [1].

The clan contains the following 12 members:

CBD_PlyG CdAMP_rec CutA1 DUF190 DUF2007 DUF2179 DUF3240 HisG_C Nit_Regul_Hom NRho P-II Rhomboid_N

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(341)
Full
(4587)
Representative proteomes UniProt
(18707)
RP15
(632)
RP35
(2116)
RP55
(4541)
RP75
(7632)
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PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(341)
Full
(4587)
Representative proteomes UniProt
(18707)
RP15
(632)
RP35
(2116)
RP55
(4541)
RP75
(7632)
Alignment:
Format:
Order:
Sequence:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(341)
Full
(4587)
Representative proteomes UniProt
(18707)
RP15
(632)
RP35
(2116)
RP55
(4541)
RP75
(7632)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_1550 (release 16.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD
Number in seed: 341
Number in full: 4587
Average length of the domain: 73.9 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 24.47 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.5 23.5
Trusted cut-off 23.6 23.9
Noise cut-off 23.4 23.2
Model length: 73
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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Structures

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 HisG_C domain has been found. There are 50 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0D2F1R3 View 3D Structure Click here
A0A0H3H0I5 View 3D Structure Click here
A0A175W0H8 View 3D Structure Click here
A0A1C1CE75 View 3D Structure Click here
A0A1D6I6V0 View 3D Structure Click here
A0JVK4 View 3D Structure Click here
A0KKB9 View 3D Structure Click here
A1A1J3 View 3D Structure Click here
A1AT72 View 3D Structure Click here
A1BIW8 View 3D Structure Click here
A1R5S0 View 3D Structure Click here
A1SVD5 View 3D Structure Click here
A1UHU3 View 3D Structure Click here
A3N3V7 View 3D Structure Click here
A3QF15 View 3D Structure Click here
A4FBW8 View 3D Structure Click here
A4SCX0 View 3D Structure Click here
A4X642 View 3D Structure Click here
A4YI31 View 3D Structure Click here
A5D3N6 View 3D Structure Click here
A5G6I5 View 3D Structure Click here
A6L2V6 View 3D Structure Click here
A6LAM0 View 3D Structure Click here
A6TBC2 View 3D Structure Click here
A6UTA7 View 3D Structure Click here
A8AAI4 View 3D Structure Click here
A8H5D9 View 3D Structure Click here
A8ZXG7 View 3D Structure Click here
B1I190 View 3D Structure Click here
B1KRG9 View 3D Structure Click here
B2FPL8 View 3D Structure Click here
B2GGU8 View 3D Structure Click here
B2VFL7 View 3D Structure Click here
B3E6L6 View 3D Structure Click here
B4ET04 View 3D Structure Click here
B4S561 View 3D Structure Click here
B4SCC0 View 3D Structure Click here
B5YJ68 View 3D Structure Click here
B6YQ21 View 3D Structure Click here
B8DQ42 View 3D Structure Click here