Summary: SNO glutamine amidotransferase family
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SNO glutamine amidotransferase family Provide feedback
This family and its amidotransferase domain was first described in . It is predicted that members of this family are involved in the pyridoxine biosynthetic pathway, based on the proximity and co-regulation of the corresponding genes and physical interaction between the members of PF01174 and PF01680 .
Galperin MY, Koonin EV; , Mol Microbiol 1997;24:443-445.: Sequence analysis of an exceptionally conserved operon suggests enzymes for a new link between histidine and purine biosynthesis. PUBMED:9159529 EPMC:9159529
Padilla PA, Fuge EK, Crawford ME, Errett A, Werner-Washburne M; , J Bacteriol 1998;180:5718-5726.: The highly conserved, coregulated SNO and SNZ gene families in Saccharomyces cerevisiae respond to nutrient limitation. PUBMED:9791124 EPMC:9791124
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002161
Members of this family are involved in the pyridoxine biosynthetic pathway [PUBMED:8955308, PUBMED:9791124]. The regulation of cellular growth and proliferation in response to environmental cues is critical for development and the maintenance of viability in all organisms. In unicellular organisms, such as the budding yeast Saccharomyces cerevisiae (Baker's yeast), growth and proliferation are regulated by nutrient availability.
Pyridoxal 5'-phosphate (PLP) is synthesized by the PdxA/PdxJ pathway in some species (mostly within the gamma subdivision of the proteobacteria) and by the Pdx1/Pdx2 pathway in most other organisms. This family describes PdxT, the glutaminase subunit of the PLP synthase. It is involved in the hydrolysis of glutamine to glutamate and ammonia, channeling an ammonia molecule to PdxS.
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Most members of this clan are glutaminase enzymes. This superfamily is shown to be related in . The clan also contains the DJ-1/PfpI family that includes the peptidase PfpI that has a catalytic Cys-His-Glu triad that differs from the class I GAT Cys-His-Glu triad.
The clan contains the following 13 members:BPL_N DJ-1_PfpI DUF1355 DUF4066 GATase GATase_3 GATase_5 Glyco_hydro_42M HTS Peptidase_C26 Peptidase_S51 SNO ThuA
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Author:||Belitsky B, Finn RD, Bateman A|
|Number in seed:||4|
|Number in full:||1876|
|Average length of the domain:||181.00 aa|
|Average identity of full alignment:||43 %|
|Average coverage of the sequence by the domain:||94.15 %|
|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:||14|
|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 SNO domain has been found. There are 30 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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