3K7D

C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF08335	e3k7dA4	A: alpha bundles	X: Four-helical up-and-down bundle	H: HEPN	T: Nucleotidyltransferase substrate binding subunit/domain	F: PF08335	ECOD (1.6)
A	PF03710	e3k7dA3	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: PF03710	ECOD (1.6)
B	PF08335	e3k7dB4	A: alpha bundles	X: Four-helical up-and-down bundle	H: HEPN	T: Nucleotidyltransferase substrate binding subunit/domain	F: PF08335	ECOD (1.6)
B	PF03710	e3k7dB3	A: a+b three layers	X: Nucleotidyltransferase-like	H: Nucleotidyltransferase (From Topology)	T: Nucleotidyltransferase	F: PF03710	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.120.1510	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)		CATH (4.3.0)
A	3.30.460.10	Alpha Beta	2-Layer Sandwich	Beta Polymerase	domain 2	CATH (4.3.0)
A	1.20.120.330	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Nucleotidyltransferases domain 2	CATH (4.3.0)
B	1.20.120.1510	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)		CATH (4.3.0)
B	3.30.460.10	Alpha Beta	2-Layer Sandwich	Beta Polymerase	domain 2	CATH (4.3.0)
B	1.20.120.330	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Nucleotidyltransferases domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF08335	GlnD PII-uridylyltransferase (GlnD_UR_UTase)	GlnD PII-uridylyltransferase	-	Family
A, B	PF03710	Glutamate-ammonia ligase adenylyltransferase (GlnE)	Glutamate-ammonia ligase adenylyltransferase	Conserved repeated domain found in GlnE proteins. These proteins adenylate and deadenylate glutamine synthases: ATP + {L-Glutamate:ammonia ligase (ADP-forming)} = Diphosphate + Adenylyl-{L-Glutamate:Ammonia ligase (ADP-forming)}. The family is rela ...	Conserved repeated domain found in GlnE proteins. These proteins adenylate and deadenylate glutamine synthases: ATP + {L-Glutamate:ammonia ligase (ADP-forming)} = Diphosphate + Adenylyl-{L-Glutamate:Ammonia ligase (ADP-forming)}. The family is related to the Pfam:PF01909 domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Glutamate-ammonia-ligase adenylyltransferase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding adenylyltransferase activity [glutamate-ammonia-ligase] adenylyltransferase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups catalytic activity, acting on a protein [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase activity	regulation of cellular process oxoacid metabolic process amino acid metabolic process organic acid metabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process regulation of primary metabolic process organic substance metabolic process cellular ketone metabolic process regulation of small molecule metabolic process small molecule metabolic process regulation of biological process organonitrogen compound metabolic process regulation of cellular ketone metabolic process regulation of cellular process oxoacid metabolic process amino acid metabolic process organic acid metabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process regulation of primary metabolic process organic substance metabolic process cellular ketone metabolic process regulation of small molecule metabolic process small molecule metabolic process regulation of biological process organonitrogen compound metabolic process regulation of cellular ketone metabolic process regulation of cellular amino acid metabolic process regulation of amine metabolic process cellular metabolic process biological regulation carboxylic acid metabolic process primary metabolic process regulation of cellular metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process amine metabolic process metabolic process cellular process regulation of metabolic process regulation of glutamine family amino acid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR043519	Nucleotidyltransferase superfamily	Homologous Superfamily
A, B	IPR023057	Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme	Family
A, B	IPR005190	Glutamate-ammonia ligase adenylyltransferase, repeated domain	Domain
A, B	IPR013546	PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase	Domain

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 R01GM133198.