2F2A

Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Gln

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2f2aa_	Alpha and beta proteins (a/b)	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Amidase signature (AS) enzymes	Glutamyl-tRNA(Gln) amidotransferase subunit A	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
B	d2f2ab1	All alpha proteins	GatB/YqeY motif	GatB/YqeY motif	GatB/GatE C-terminal domain-like	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B, GatB, C-terminal domain	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
B	d2f2ab2	Alpha and beta proteins (a+b)	Glutamine synthetase/guanido kinase	Glutamine synthetase/guanido kinase	GatB/GatE catalytic domain-like	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B, GatB, N-terminal domain	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
C	d2f2ac_	All alpha proteins	Non-globular all-alpha subunits of globular proteins	Glu-tRNAGln amidotransferase C subunit	Glu-tRNAGln amidotransferase C subunit	Glu-tRNAGln amidotransferase C subunit, GatC	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Amidase signature (AS) enzymes	8028092	4002446	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Amidase signature (AS) enzymes	8040471	3001251	SCOP2 (2022-06-29)
B	SCOP2 Family	GatB/GatE C-terminal domain-like	8028094	4001495	SCOP2 (2022-06-29)
B	SCOP2 Family	GatB/GatE catalytic domain-like	8028096	4003972	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	GatB/YqeY motif	8040473	3001497	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Glutamine synthetase/guanido kinase	8040475	3000676	SCOP2 (2022-06-29)
C	SCOP2 Family	GatC-like	8028098	4001576	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	GatC-like	8040477	3001870	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Amidase	e2f2aA1	A: a/b three-layered sandwiches	X: Amidase signature (AS) enzymes (From Topology)	H: Amidase signature (AS) enzymes (From Topology)	T: Amidase signature (AS) enzymes	F: Amidase	ECOD (1.6)
B	GatB_Yqey	e2f2aB1	A: alpha arrays	X: ERP29 C domain-like	H: GatB/GatE C-terminal domain (From Topology)	T: GatB/GatE C-terminal domain	F: GatB_Yqey	ECOD (1.6)
B	GatB_N	e2f2aB2	A: a+b two layers	X: Glutamine synthetase-like	H: Glutamine synthetase/guanido kinase (From Topology)	T: Glutamine synthetase/guanido kinase	F: GatB_N	ECOD (1.6)
C	Glu-tRNAGln	e2f2aC1	A: extended segments	X: Glu-tRNAGln amidotransferase C subunit (From Topology)	H: Glu-tRNAGln amidotransferase C subunit (From Topology)	T: Glu-tRNAGln amidotransferase C subunit	F: Glu-tRNAGln	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1300.10	Alpha Beta	Alpha-Beta Complex	Amidase signature (AS) enzymes	Amidase signature (AS) domain	CATH (4.3.0)
C	1.10.20.60	Mainly Alpha	Orthogonal Bundle	Histone, subunit A	Glu-tRNAGln amidotransferase C subunit, N-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01425	Amidase (Amidase)	Amidase	-	Family
B	PF02637	GatB domain (GatB_Yqey)	GatB domain	This domain is found in GatB. It is about 140 amino acid residues long. This domain is found at the C terminus of GatB Swiss:O30509 which transamidates Glu-tRNA to Gln-tRNA.	Domain
B	PF02934	GatB/GatE catalytic domain (GatB_N)	GatB/GatE catalytic domain	This domain is found in the GatB and GatE proteins [1].	Domain
C	PF02686	Glu-tRNAGln amidotransferase C subunit (GatC)	Glu-tRNAGln amidotransferase C subunit	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Glutamyl-tRNA(Gln) amidotransferase subunit A	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding carbon-nitrogen ligase activity, with glutamine as amido-N-donor catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid catalytic activity, acting on a tRNA glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity	biosynthetic process metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process translation gene expression macromolecule biosynthetic process	protein-containing complex catalytic complex glutamyl-tRNA(Gln) amidotransferase complex intracellular protein-containing complex
B	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding carbon-nitrogen ligase activity, with glutamine as amido-N-donor catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid catalytic activity, acting on a tRNA glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity	biosynthetic process metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process translation gene expression macromolecule biosynthetic process	-
C	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding carbon-nitrogen ligase activity, with glutamine as amido-N-donor catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid catalytic activity, acting on a tRNA glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity	biological regulation regulation of biological quality regulation of translational fidelity biosynthetic process metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process translation gene expression macromolecule biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036928	Amidase signature (AS) superfamily	Homologous Superfamily
A	IPR004412	Glutamyl-tRNA(Gln) amidotransferase A subunit	Family
A	IPR000120	Amidase	Family
A	IPR023631	Amidase signature domain	Domain
A	IPR020556	Amidase, conserved site	Conserved Site
B	IPR006075	Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic	Domain
B	IPR042114	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C-terminal, domain 1	Homologous Superfamily
B	IPR003789	Aspartyl/glutamyl-tRNA amidotransferase subunit B-like	Homologous Superfamily
B	IPR017959	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E	Family
B	IPR023168	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, C-terminal, domain 2	Homologous Superfamily
B	IPR018027	Asn/Gln amidotransferase	Domain
B	IPR017958	Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site	Conserved Site
B	IPR004413	Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B	Family
B	IPR014746	Glutamine synthetase/guanido kinase, catalytic domain	Homologous Superfamily
C	IPR003837	Glu-tRNAGln amidotransferase C subunit	Family
C	IPR036113	Glu-tRNAGln amidotransferase superfamily, subunit C	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.