4YFY

X-ray structure of the Viof N-formyltransferase from Providencia alcalifaciens O30 in complex with THF and TDP-Qui4N

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	PRK07579	e4yfyA1	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
A	Formyl_trans_N	e4yfyA2	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
B	PRK07579	e4yfyB2	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
B	Formyl_trans_N	e4yfyB1	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
B	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF18216	N-formyltransferase dimerization C-terminal domain (N_formyltrans_C)	N-formyltransferase dimerization C-terminal domain	This is the C-terminal domain of N-formyltransferase found in Francisella tularensis. N-formylated sugars are observed on O-antigens of pathogenic Gram-negative bacteria. This C-terminal domain is responsible for dimerization. In particular, the beta ...	This is the C-terminal domain of N-formyltransferase found in Francisella tularensis. N-formylated sugars are observed on O-antigens of pathogenic Gram-negative bacteria. This C-terminal domain is responsible for dimerization. In particular, the beta hairpin motif present in the domain helps create a subunit-subunit interface. The dimeric interface is characterized by a hydrophobic patch formed by Ile 195, Leu 197, Val 201, Met 203, Ile 207, Phe 223, Val 231, Val 233, Leu 235, and Leu 237 from both monomers [1].	Domain
A, B	PF00551	Formyl transferase (Formyl_trans_N)	Formyl transferase	This family includes the following members. Glycinamide ribonucleotide transformylase catalyses the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces ...	This family includes the following members. Glycinamide ribonucleotide transformylase catalyses the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	VioF	-	biosynthetic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR040660	N-formyltransferase dimerization C-terminal domain	Domain
A, B	IPR002376	Formyl transferase, N-terminal	Domain
A, B	IPR036477	Formyl transferase, N-terminal domain superfamily	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.