Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APRK07579e4yfvA1 A: beta barrelsX: FMT C-terminal domain-likeH: FMT C-terminal domain-related (From Topology)T: FMT C-terminal domain-relatedF: PRK07579ECOD (1.6)
AFormyl_trans_Ne4yfvA2 A: a/b three-layered sandwichesX: Formyltransferase (From Topology)H: Formyltransferase (From Topology)T: FormyltransferaseF: Formyl_trans_NECOD (1.6)
BPRK07579e4yfvB2 A: beta barrelsX: FMT C-terminal domain-likeH: FMT C-terminal domain-related (From Topology)T: FMT C-terminal domain-relatedF: PRK07579ECOD (1.6)
BFormyl_trans_Ne4yfvB1 A: a/b three-layered sandwichesX: Formyltransferase (From Topology)H: Formyltransferase (From Topology)T: FormyltransferaseF: Formyl_trans_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.40.50.170 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Formyl transferase, N-terminal domainCATH (4.3.0)
B3.40.50.170 Alpha Beta 3-Layer(aba) Sandwich Rossmann fold Formyl transferase, N-terminal domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF18216N-formyltransferase dimerization C-terminal domain (N_formyltrans_C)N-formyltransferase dimerization C-terminal domainThis 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
PF00551Formyl transferase (Formyl_trans_N)Formyl transferaseThis 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

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
VioF- -