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113  structures 6931  species 9  interactions 29637  sequences 151  architectures

Family: GATase (PF00117)

Summary: Glutamine amidotransferase class-I

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This is the Wikipedia entry entitled "Glutamine amidotransferase". More...

Glutamine amidotransferase Edit Wikipedia article

Glutamine amidotransferase class-I
PDB 1o1y EBI.jpg
crystal structure of putative glutamine amido transferase (tm1158) from thermotoga maritima at 1.70 a resolution
Identifiers
Symbol GATase
Pfam PF00117
Pfam clan CL0014
InterPro IPR000991
PROSITE PDOC00406
MEROPS C44
SCOP 1ea0
SUPERFAMILY 1ea0

In molecular biology, glutamine amidotransferases (GATase) are enzymes which catalyse the removal of the ammonia group from a glutamine molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This activity is found in a range of biosynthetic enzymes, including glutamine amidotransferase, anthranilate synthase component II, p-aminobenzoate, and glutamine-dependent carbamoyl-transferase (CPSase). Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. On the basis of sequence similarities two classes of GATase domains have been identified: class-I (also known as trpG-type) and class-II (also known as purF-type).[1][2] Class-I GATase domains are defined by a conserved catalytic triad consisting of cysteine, histidine and glutamate. Class-I GATase domains have been found in the following enzymes: the second component of anthranilate synthase and 4-amino-4-deoxychorismate (ADC) synthase; CTP synthase; GMP synthase; glutamine-dependent carbamoyl-phosphate synthase; phosphoribosylformylglycinamidine synthase II; and the histidine amidotransferase hisH.

References[edit]

  1. ^ Weng ML, Zalkin H (July 1987). "Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain". J. Bacteriol. 169 (7): 3023–8. PMC 212343. PMID 3298209. 
  2. ^ Nyunoya H, Lusty CJ (August 1984). "Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain". J. Biol. Chem. 259 (15): 9790–8. PMID 6086650. 

This article incorporates text from the public domain Pfam and InterPro IPR000991

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Glutamine amidotransferase class-I Provide feedback

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR017926

Glutamine amidotransferase (GATase) enzymes catalyse the removal of the ammonia group from glutamine and then transfer this group to a substrate to form a new carbon-nitrogen group [PUBMED:4355768]. The GATase domain exists either as a separate polypeptidic subunit or as part of a larger polypeptide fused in different ways to a synthase domain. Two classes of GATase domains have been identified [PUBMED:3298209, PUBMED:6086650]: class-I (also known as trpG-type or triad) and class-II (also known as purF-type or Ntn). Class-I (or type 1) GATase domains have been found in the following enzymes:

  • The second component of anthranilate synthase (AS) [PUBMED:2679363]. AS catalyzes the biosynthesis of anthranilate from chorismate and glutamine. AS is generally a dimeric enzyme: the first component can synthesize anthranilate using ammonia rather than glutamine, whereas component II provides the GATase activity [PUBMED:10449718]. In some bacteria and in fungi the GATase component of AS is part of a multifunctional protein that also catalyzes other steps of the biosynthesis of tryptophan.
  • The second component of 4-amino-4-deoxychorismate (ADC) synthase, a dimeric prokaryotic enzyme that functions in the pathway that catalyzes the biosynthesis of para-aminobenzoate (PABA) from chorismate and glutamine. The second component (gene pabA) provides the GATase activity [PUBMED:2679363].
  • CTP synthase. CTP synthase catalyzes the final reaction in the biosynthesis of pyrimidine, the ATP-dependent formation of CTP from UTP and glutamine. CTP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the C-terminal section [PUBMED:3298209].
  • GMP synthase (glutamine-hydrolyzing). GMP synthase catalyzes the ATP-dependent formation of GMP from xanthosine 5'-phosphate and glutamine. GMP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the N-terminal section [PUBMED:2982857, PUBMED:8548458].
  • Glutamine-dependent carbamoyl-phosphate synthase (GD-CPSase); an enzyme involved in both arginine and pyrimidine biosynthesis and which catalyzes the ATP-dependent formation of carbamoyl phosphate from glutamine and carbon dioxide. In bacteria GD-CPSase is composed of two subunits: the large chain (gene carB) provides the CPSase activity, while the small chain (gene carA) provides the GATase activity. In yeast the enzyme involved in arginine biosynthesis is also composed of two subunits: CPA1 (GATase), and CPA2 (CPSase). In most eukaryotes, the first three steps of pyrimidine biosynthesis are catalyzed by a large multifunctional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals). The GATase domain is located at the N-terminal extremity of this polyprotein [PUBMED:8098212].
  • Phosphoribosylformylglycinamidine synthase, an enzyme that catalyzes the fourth step in the de novo biosynthesis of purines. In some species of bacteria and rchaea, FGAM synthase II is composed of two subunits: a small chain (gene purQ) which provides the GATase activity and a large chain (gene purL) which provides the aminator activity. In eukaryotes and Gram-negative bacteria a single polypeptide (large type of purL) contains a FGAM synthethase domain and the GATase as the C-terminal domain [PUBMED:15301531].
  • Imidazole glycerol phosphate synthase subunit hisH, an enzyme that catalyzes the fifth step in the biosynthesis of histidine.
A triad of conserved Cys-His-Glu forms the active site, wherein the catalytic cysteine is essential for the amidotransferase activity [PUBMED:8548458, PUBMED:9575335]. Different structures show that the active site Cys of type 1 GATase is located at the tip of a nucleophile elbow.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Glutaminase_I (CL0014), which 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

Alignments

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(18089)
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RP35
(4699)
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(6278)
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  Seed
(134)
Full
(29637)
Representative proteomes NCBI
(26546)
Meta
(18089)
RP15
(2366)
RP35
(4699)
RP55
(6278)
RP75
(7451)
Alignment:
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  Seed
(134)
Full
(29637)
Representative proteomes NCBI
(26546)
Meta
(18089)
RP15
(2366)
RP35
(4699)
RP55
(6278)
RP75
(7451)
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External links

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Curation and family details

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Seed source: Prosite
Previous IDs: none
Type: Domain
Author: Sonnhammer ELL
Number in seed: 134
Number in full: 29637
Average length of the domain: 186.40 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 46.33 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.3 22.3
Trusted cut-off 22.3 22.3
Noise cut-off 22.2 22.2
Model length: 192
Family (HMM) version: 23
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Species distribution

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Interactions

There are 9 interactions for this family. More...

CPSase_L_D3 Anth_synt_I_N GMP_synt_C CPSase_sm_chain His_biosynth GATase CTP_synth_N Chorismate_bind CPSase_L_D2

Structures

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 GATase domain has been found. There are 113 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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