Annotations: 4IOL

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4iola_	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	automated matches	(Moorella thermoacetica ATCC 39073 ) [TaxId: 264732 ],	SCOPe (2.08)
B	d4iolb_	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	Nitrogenase iron protein-like	automated matches	(Moorella thermoacetica ATCC 39073 ) [TaxId: 264732 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	FTHFS	e4iolA1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: FTHFS	ECOD (1.6)
B	FTHFS	e4iolB1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: FTHFS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
A	3.30.1510.10	Alpha Beta	2-Layer Sandwich	Domain 2, N(10)-formyltetrahydrofolate synthetase	Domain 2, N(10)-formyltetrahydrofolate synthetase	CATH (4.3.0)
A	3.10.410.10	Alpha Beta	Roll	Formyltetrahydrofolate synthetase	domain 3	CATH (4.3.0)
B	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
B	3.30.1510.10	Alpha Beta	2-Layer Sandwich	Domain 2, N(10)-formyltetrahydrofolate synthetase	Domain 2, N(10)-formyltetrahydrofolate synthetase	CATH (4.3.0)
B	3.10.410.10	Alpha Beta	Roll	Formyltetrahydrofolate synthetase	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01268	Formate--tetrahydrofolate ligase (FTHFS)	Formate--tetrahydrofolate ligase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Formate--tetrahydrofolate ligase	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 formate-tetrahydrofolate ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity	folic acid-containing compound metabolic process cellular metabolic process tetrahydrofolate interconversion metabolic process cellular process small molecule metabolic process tetrahydrofolate metabolic process pteridine-containing compound metabolic process cellular modified amino acid metabolic process one-carbon metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR020628	Formate-tetrahydrofolate ligase, FTHFS, conserved site	Conserved Site
A, B	IPR000559	Formate-tetrahydrofolate ligase, FTHFS	Family
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	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.