The domain within your query sequence starts at position 166 and ends at position 468; the E-value for the GATase_5 domain shown below is 6.88e-120.

VPRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAIRLDTFRGVAFVGGFSYAD
VLGSAKGWAAAVTFNPQAREELGRFRRRPDTFSLGVCNGCQLLALLGWVGSDPSEEQAEP
GQDSQPTQPGLLLRHNLSGRFESRWATVRVEPGPALMLRGMEGSVLPVWSAHGEGQAGKA
GEGLQAGAGAGPEGTWPSLSSPSLPGYMAFSSPELQAKIEAKGLVPLHWADDDGNPTEQY
PLNPNGSPGGIAGICSQDGRHLALMPHPERAVRLWQWAWRPSPFDVLPTSPWLQLFINAR
NWT

GATase_5

CobB/CobQ-like glutamine amidotransferase domain

• SMART accession number: SM01211
• Description: -

There are 21508 GATase_5 domains in 21508 proteins in SMART's nrdb database.

Literature (relevant references for this domain)

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

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	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)

• PFAM: GATase_5