GATase_5CobB/CobQ-like glutamine amidotransferase domain |
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| SMART accession number: | SM01211 |
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| Description: | - |
| Family alignment: |
There are 21508 GATase_5 domains in 21508 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Taxonomic distribution of proteins containing GATase_5 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with GATase_5 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing GATase_5 domain in the selected taxonomic class.
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Galperin MY, Grishin NV
- The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotinsynthetase.
- Proteins. 2000; 41: 238-47
- Display abstract
Phosphotransacetylases of Escherichia coli and several other bacteria contain an additional 350-aa N-terminal fragment that is not required forphosphotransacetylase activity. Sequence analysis of this fragment revealed that it is closely related to a family of ATP-dependent enzymes that also includesdethiobiotin synthetase and the synthetase domains of two amidotransferasesinvolved in cobalamin biosynthesis, cobyrinic acid a,c-diamide synthase (CobB)and cobyric acid synthase (CobQ). Further database searches showed that thisenzyme family is also related to the MinD family of ATPases involved inregulation of cell division in bacteria and archaea. Analysis of sequenceconservation in the members of this enzyme family using the structure ofdethiobiotin synthetase active site as a guide allowed us to suggest a model for the interaction of CobB and CobQ with their respective substrates. CobB and CobQ were also found to contain unusual Triad family (class I) glutamineamidotransferase domains with conserved Cys and His residues, but lacking the Gluresidue of the catalytic triad. These results should help in understanding theenzymology of cobalamin biosynthesis and in resolving the role ofphosphotransacetylase in regulation of the carbon flow to and from acetate.
- Structure (3D structures containing this domain)
3D Structures of GATase_5 domains in PDB
PDB code Main view Title 1t3t 
Structure of Formylglycinamide synthetase 3d54 
Stucture of PurLQS from Thermotoga maritima 3ugj 
Formyl Glycinamide ribonucletide amidotransferase from Salmonella Typhimurum: Role of the ATP complexation and glutaminase domain in catalytic coupling 3ujn 
Formyl Glycinamide Ribonucleotide Amidotransferase from Salmonella Typhimurium : Role of the ATP complexation and glutaminase domain in catalytic coupling 3umm 
Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: Role of the ATP complexation and glutaminase domain in catalytic coupling 4l78 
Xenon Trapping and Statistical Coupling Analysis Uncover Regions Important for Structure and Function of Multidomain Protein StPurL 4lgy 
Importance of Hydrophobic Cavities in Allosteric Regulation of Formylglycinamide Synthetase: Insight from Xenon Trapping and Statistical Coupling Analysis 4mgh 
Importance of Hydrophobic Cavities in Allosteric Regulation of Formylglycinamide Synthetase: Insight from Xenon Trapping and Statistical Coupling Analysis 4r7g 
4R7G - Links (links to other resources describing this domain)
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PFAM GATase_5