Annotations: 2VXO

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8065931	3001405	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8065931	3001405	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	GMP_synt_C	e2vxoB2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: GMP synthetase C-terminal dimerisation domain (From Topology)	T: GMP synthetase C-terminal dimerisation domain	F: GMP_synt_C	ECOD (1.6)
B	tRNA_Me_trans_1st	e2vxoB1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: tRNA_Me_trans_1st	ECOD (1.6)
B	GATase	e2vxoB3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: GATase	ECOD (1.6)
A	GMP_synt_C	e2vxoA2	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: GMP synthetase C-terminal dimerisation domain (From Topology)	T: GMP synthetase C-terminal dimerisation domain	F: GMP_synt_C	ECOD (1.6)
A	tRNA_Me_trans_1st	e2vxoA3	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: tRNA_Me_trans_1st	ECOD (1.6)
A	GATase	e2vxoA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: GATase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (4.3.0)
B	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (4.3.0)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00117	Glutamine amidotransferase class-I (GATase)	Glutamine amidotransferase class-I	-	Domain
A, B	PF00958	GMP synthase C terminal domain (GMP_synt_C)	GMP synthase C terminal domain	GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases Swiss:P49915 EC:6.3.5.2. In prokaryotes this domain mediates dimerisation. Eukaryotic GMP ...	GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases Swiss:P49915 EC:6.3.5.2. In prokaryotes this domain mediates dimerisation. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains.	Domain
A, B	PF02540	NAD synthase (NAD_synthase)	NAD synthase	NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	GMP SYNTHASE [GLUTAMINE-HYDROLYZING]	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 GMP synthase (glutamine-hydrolyzing) activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity GMP synthase activity	nucleoside phosphate metabolic process purine ribonucleoside monophosphate biosynthetic process primary metabolic process nucleobase-containing compound biosynthetic process nucleoside monophosphate biosynthetic process nucleobase-containing compound metabolic process purine nucleoside monophosphate biosynthetic process purine ribonucleoside monophosphate metabolic process biosynthetic process ribonucleoside monophosphate metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process purine nucleoside monophosphate metabolic process phosphate-containing compound metabolic process nucleoside phosphate metabolic process purine ribonucleoside monophosphate biosynthetic process primary metabolic process nucleobase-containing compound biosynthetic process nucleoside monophosphate biosynthetic process nucleobase-containing compound metabolic process purine nucleoside monophosphate biosynthetic process purine ribonucleoside monophosphate metabolic process biosynthetic process ribonucleoside monophosphate metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process purine nucleoside monophosphate metabolic process phosphate-containing compound metabolic process nucleoside phosphate biosynthetic process metabolic process cellular process small molecule metabolic process ribonucleoside monophosphate biosynthetic process nucleoside monophosphate metabolic process phosphorus metabolic process ribose phosphate metabolic process nucleotide biosynthetic process carbohydrate derivative metabolic process purine ribonucleotide biosynthetic process ribonucleotide biosynthetic process purine nucleotide metabolic process ribonucleotide metabolic process purine-containing compound biosynthetic process GMP metabolic process ribose phosphate biosynthetic process carbohydrate derivative biosynthetic process GMP biosynthetic process nucleotide metabolic process purine-containing compound metabolic process purine ribonucleotide metabolic process purine nucleotide biosynthetic process glutamine metabolic process oxoacid metabolic process carboxylic acid metabolic process amino acid metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process glutamine family amino acid metabolic process proteinogenic amino acid metabolic process nucleobase biosynthetic process purine nucleobase metabolic process purine nucleobase biosynthetic process nucleobase metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029062	Class I glutamine amidotransferase-like	Homologous Superfamily
A, B	IPR022310	NAD/GMP synthase	Domain
A, B	IPR004739	GMP synthase, glutamine amidotransferase	Domain
A, B	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily
A, B	IPR001674	GMP synthase, C-terminal	Domain
A, B	IPR017926	Glutamine amidotransferase	Domain
A, B	IPR025777	GMP synthetase ATP pyrophosphatase domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P49915	acute myeloid leukemia gastric cancer osteosarcoma subependymal giant cell astrocytoma adenoma gastric carcinoma ovarian cancer cancer hepatocellular carcinoma partial epilepsy

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.