4B4U

Crystal structure of Acinetobacter baumannii N5, N10- methylenetetrahydrofolate dehydrogenase-cyclohydrolase (FolD) complexed with NADP cofactor

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d4b4ua2	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	SCOPe (2.08)
A	d4b4ua1	Alpha and beta proteins (a/b)	Aminoacid dehydrogenase-like, N-terminal domain	Aminoacid dehydrogenase-like, N-terminal domain	automated matches	automated matches	(Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	SCOPe (2.08)
B	d4b4ub2	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	SCOPe (2.08)
B	d4b4ub1	Alpha and beta proteins (a/b)	Aminoacid dehydrogenase-like, N-terminal domain	Aminoacid dehydrogenase-like, N-terminal domain	automated matches	automated matches	(Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	SCOPe (2.08)
B	d4b4ub3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841 ) [TaxId: 575584 ],	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	THF_DHG_CYH_C	e4b4uA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: THF_DHG_CYH_C	ECOD (1.6)
A	THF_DHG_CYH	e4b4uA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Aminoacid dehydrogenase-like, N-terminal domain	F: THF_DHG_CYH	ECOD (1.6)
B	THF_DHG_CYH_C	e4b4uB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: THF_DHG_CYH_C	ECOD (1.6)
B	THF_DHG_CYH	e4b4uB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Aminoacid dehydrogenase-like, N-terminal domain	F: THF_DHG_CYH	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	3.40.50.10860	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Leucine Dehydrogenase, chain A, domain 1	CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	3.40.50.10860	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Leucine Dehydrogenase, chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02882	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain (THF_DHG_CYH_C)	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain	-	Domain
A, B	PF00763	Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain (THF_DHG_CYH)	Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	BIFUNCTIONAL PROTEIN FOLD	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines cyclohydrolase activity methenyltetrahydrofolate cyclohydrolase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds methylenetetrahydrofolate dehydrogenase (NADP+) activity oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-NH group of donors methylenetetrahydrofolate dehydrogenase [NAD(P)+] activity binding nucleoside phosphate binding organic cyclic compound binding hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines cyclohydrolase activity methenyltetrahydrofolate cyclohydrolase activity hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds methylenetetrahydrofolate dehydrogenase (NADP+) activity oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-NH group of donors methylenetetrahydrofolate dehydrogenase [NAD(P)+] activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding	nucleoside phosphate metabolic process cellular metabolic process nucleotide biosynthetic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process biosynthetic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process nucleoside phosphate metabolic process cellular metabolic process nucleotide biosynthetic process primary metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process biosynthetic process organophosphate metabolic process nucleobase-containing small molecule metabolic process organophosphate biosynthetic process purine-containing compound biosynthetic process phosphate-containing compound metabolic process nucleoside phosphate biosynthetic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process purine nucleotide biosynthetic process oxoacid metabolic process cellular biosynthetic process sulfur amino acid metabolic process aspartate family amino acid biosynthetic process aspartate family amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process sulfur compound metabolic process methionine biosynthetic process small molecule biosynthetic process carboxylic acid metabolic process L-amino acid biosynthetic process methionine metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process sulfur compound biosynthetic process proteinogenic amino acid biosynthetic process sulfur amino acid biosynthetic process alpha-amino acid biosynthetic process folic acid-containing compound metabolic process tetrahydrofolate interconversion tetrahydrofolate metabolic process pteridine-containing compound metabolic process cellular modified amino acid metabolic process one-carbon metabolic process imidazole-containing compound metabolic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process L-histidine metabolic process L-histidine biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR046346	Aminoacid dehydrogenase-like, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain	Domain
A, B	IPR020630	Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain	Domain
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR020867	Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site	Conserved Site
A, B	IPR000672	Tetrahydrofolate dehydrogenase/cyclohydrolase	Family

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.