Summary: CobB/CobQ-like glutamine amidotransferase domain
CobB/CobQ-like glutamine amidotransferase domain Provide feedback
No Pfam abstract.
Galperin MY, Grishin NV; , Proteins 2000;41:238-247.: The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase. PUBMED:10966576 EPMC:10966576
Internal database links
|Similarity to PfamA using HHSearch:||DJ-1_PfpI GATase Peptidase_S51 SNO Peptidase_C26 GATase_5|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011698This group of enzymes was suggested to be related to the MinD family of ATPases involved in regulation of cell division in bacteria and archaea [PUBMED:10966576]. Further sequence analysis suggests a model for the interaction of CobB and CobQ with their respective substrates [PUBMED:10966576]. CobB and CobQ were also found to contain unusual Triad family (class I) glutamine amidotransferase domains with conserved Cys and His residues, but lacking the Glu residue of the catalytic triad [PUBMED:10966576].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||catalytic activity (GO:0003824)|
|Biological process||cobalamin biosynthetic process (GO:0009236)|
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Curation and family details
|Number in seed:||88|
|Number in full:||5307|
|Average length of the domain:||155.60 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||37.14 %|
|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:||9|
|Download:||download the raw HMM for this family|
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