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5  structures 219  species 0  interactions 240  sequences 6  architectures

Family: PanZ (PF12568)

Summary: Acetyltransferase (GNAT) domain, PanZ

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Acetyltransferase (GNAT) domain, PanZ Provide feedback

This domain family is found in bacteria, and is approximately 40 amino acids in length. The proteins in this family are members of the acetyltransferases of the GNAT family. Family members such as PanZ has been shown to be involved in the biosynthesis of Coenzyme A (CoA). CoA is a ubiquitous and essential cofactor, synthesized from the precursor pantothenate. In all organisms, the final step in pantothenate biosynthesis relies on the presence of beta-alanine, which comes from different sources in bacteria, yeast, and plants. In bacteria, beta-alanine is derived by the action of alpha-decarboxylase (ADC) enzyme. PanZ promotes the activation of the zymogen, PanD, to form aspartate alpha-decarboxylase (ADC) in a CoA-dependent manner. Thereby, playing an essential role in the biosynthetic pathway to pantothenate and the regulation of CoA biosynthesis. Structure and function studies show that direct interaction of PanD with the PanZ Arg43-Leu46 loop promotes PanD to adopt a reactive conformation, which leads to activation [1].

Literature references

  1. Monteiro DC, Patel V, Bartlett CP, Nozaki S, Grant TD, Gowdy JA, Thompson GS, Kalverda AP, Snell EH, Niki H, Pearson AR, Webb ME;, Chem Biol. 2015;22:492-503.: The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A. PUBMED:25910242 EPMC:25910242

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR040448

This entry represents the GNAT domain found in PanZ.

PanD is a l-aspartate alpha-decarboxylase involved in the biosynthesis of pantothenate, the precursor of coenzyme A (CoA). PanD is synthesised as pro-PanD, which undergoes auto-proteolytic cleavage to generate active PanD. PanM binds to and activates PanD by stabilising pro-PanD in an autocleavage-prone conformation [ PUBMED:22497218 ]. PanM acts as an acetyl-CoA sensor that can trigger the maturation of pro-PanD, but lacks acetyltransferase activity [ PUBMED:22782525 ]. The regulation of PanD by PanZ allows enterobacterial species to closely regulate production of beta-alanine and hence pantothenate in response to metabolic demand [ PUBMED:23170229 ]. Structure and function studies show that direct interaction of PanD with the PanZ Arg43-Leu46 loop promotes PanD to adopt a reactive conformation, which leads to activation [ PUBMED:25910242 ].

Domain organisation

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

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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...

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

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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...


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.

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Curation and family details

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Curation View help on the curation process

Seed source: Prosite
Previous IDs: DUF3749;
Type: Domain
Sequence Ontology: SO:0000417
Author: Gavin OL, Bateman A
Number in seed: 6
Number in full: 240
Average length of the domain: 121.2 aa
Average identity of full alignment: 30 %
Average coverage of the sequence by the domain: 87.07 %

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 22.0 22.0
Trusted cut-off 22.0 22.0
Noise cut-off 21.9 21.9
Model length: 128
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

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Colour assignments

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


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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 PanZ domain has been found. There are 5 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
A0A0H3H464 View 3D Structure Click here
P37613 View 3D Structure Click here
Q32AS4 View 3D Structure Click here
Q7CPJ9 View 3D Structure Click here
Q9HU40 View 3D Structure Click here