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44  structures 5881  species 0  interactions 7005  sequences 27  architectures

Family: ArgJ (PF01960)

Summary: ArgJ family

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This is the Wikipedia entry entitled "ArgJ protein family". More...

ArgJ protein family Edit Wikipedia article

PDB 1vz7 EBI.jpg
ornithine acetyltransferase (orf6 gene product - clavulanic acid biosynthesis) from streptomyces clavuligerus

In molecular biology, members of the ArgJ protein family are bifunctional protein that catalyses the first (EC and fifth steps (EC in arginine biosynthesis.[1] The structure has been determined for glutamate N-acetyltransferase 2 (ornithine acetyltransferase), an ArgJ-like protein from Streptomyces clavuligerus.[2]


  1. ^ Sakanyan V, Charlier D, Legrain C, Kochikyan A, Mett I, Pierard A, Glansdorff N (March 1993). "Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase". J. Gen. Microbiol. 139 (3): 393–402. doi:10.1099/00221287-139-3-393. PMID 8473852.
  2. ^ Elkins JM, Kershaw NJ, Schofield CJ (January 2005). "X-ray crystal structure of ornithine acetyltransferase from the clavulanic acid biosynthesis gene cluster". Biochem. J. 385 (Pt 2): 565–73. doi:10.1042/BJ20040814. PMC 1134730. PMID 15352873.
This article incorporates text from the public domain Pfam and InterPro: IPR002813

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ArgJ family Provide feedback

Members of the ArgJ family catalyse the first EC: and fifth steps EC: in arginine biosynthesis.

Literature references

  1. Sakanyan V, Charlier D, Legrain C, Kochikyan A, Mett I, Pierard A, Glansdorff N; , J Gen Microbiol 1993;139:393-402.: Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase. PUBMED:8473852 EPMC:8473852

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002813

ArgJ (also known as Ornithine acetyltransferase/OAT) is a bifunctional protein that catalyses the first EC and fifth steps EC in arginine biosynthesis [ PUBMED:8473852 ], coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. The structure has been determined for glutamate N-acetyltransferase 2 (ornithine acetyltransferase; EC ), an ArgJ-like protein from Streptomyces clavuligerus [ PUBMED:15352873 ].

Members of this family may experience feedback inhibition by L-arginine. The active enzyme is a heterotetramer of two alpha and two beta chains, where the alpha and beta chains are the result of autocatalytic cleavage. OATs found in the clavulanic acid biosynthesis gene cluster catalyze the fifth step only, and may utilize acetyl acceptors other than glutamate [ PUBMED:15375131 , PUBMED:15352873 , PUBMED:12633501 , PUBMED:8473852 , PUBMED:4365537 , PUBMED:15937278 ].

Gene Ontology

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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 DmpA_ArgJ (CL0635), which has the following description:

This superfamily includes the ArgJ protein and members of peptidase family S58. According to SCOP these proteins have a fold which resembles but is unrelated to that of the NTN hydrolases.

The clan contains the following 5 members:

ArgJ Ceramidase_alk MoCoBD_1 MoCoBD_2 Peptidase_S58


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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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

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.

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Seed source: Enright A
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Enright A , Ouzounis C , Bateman A
Number in seed: 648
Number in full: 7005
Average length of the domain: 377.60 aa
Average identity of full alignment: 40 %
Average coverage of the sequence by the domain: 93.28 %

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 32.0 32.0
Trusted cut-off 32.0 32.0
Noise cut-off 31.9 31.8
Model length: 375
Family (HMM) version: 21
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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 ArgJ domain has been found. There are 44 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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