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Amidinotransferase Provide feedback
This family contains glycine ( EC:126.96.36.199) and inosamine ( EC:188.8.131.52) amidinotransferases, enzymes involved in creatine and streptomycin biosynthesis respectively. This family also includes arginine deiminases, EC:184.108.40.206. These enzymes catalyse the reaction: arginine + H2O <=> citrulline + NH3. Also found in this family is the Streptococcus anti tumour glycoprotein  (P16962).
Humm A, Fritsche E, Steinbacher S, Huber R; , EMBO J 1997;16:3373-3385.: Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. PUBMED:9218780 EPMC:9218780
Pissowotzki K, Mansouri K, Piepersberg W; , Mol Gen Genet 1991;231:113-123.: Genetics of streptomycin production in Streptomyces griseus: molecular structure and putative function of genes strELMB2N. PUBMED:1661369 EPMC:1661369
D'Hooghe I, Vander Wauven C, Michiels J, Tricot C, de Wilde P, Vanderleyden J, Stalon V; , J Bacteriol 1997;179:7403-7409.: The arginine deiminase pathway in Rhizobium etli: DNA sequence analysis and functional study of the arcABC genes. PUBMED:9393705 EPMC:9393705
Kanaoka M, Fukita Y, Taya K, Kawanaka C, Negoro T, Agui H; , Jpn J Cancer Res 1987;78:1409-1414.: Antitumor activity of streptococcal acid glycoprotein produced by Streptococcus pyogenes Su. PUBMED:3123442 EPMC:3123442
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003198
This family contains glycine and inosamine amidinotransferases, enzymes which are involved in creatine and streptomycin biosynthesis respectively. This family also includes arginine deiminases, which catalyse the reversible reaction:
The Streptococcus anti-tumour glycoprotein is also found in this family [PUBMED:9218780].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Molecular function||hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines (GO:0016813)|
- 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 contains a number of related enzymes such as AstB, peptidyl-arginine deiminase, arginine deiminase and amidinotransferase [1,2].
The clan contains the following 4 members:Amidinotransf AstB PAD PAD_porph
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
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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:||Pfam-B_5784 (release 5.2) and Pfam-B_1850 (release 5.5)|
|Author:||Mian N, Bateman A|
|Number in seed:||55|
|Number in full:||3546|
|Average length of the domain:||321.90 aa|
|Average identity of full alignment:||24 %|
|Average coverage of the sequence by the domain:||89.76 %|
|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:||12|
|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 Amidinotransf domain has been found. There are 60 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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