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InterPro: IPR002376 Formyl transferase, N-terminal

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Matches:

5352 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Architectures
Accession List
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Accession

IPR002376 Formyl_transf_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.50.170	Formyl_transf_N	5185
Pfam	PF00551	Formyl_trans_N	5213
SuperFamily	SSF53328	formyl_transf	5326
Signatures in BioMart

InterPro Relationships Help

Found in

IPR004607 Phosphoribosylglycinamide formyltransferase
IPR004810 Formyltetrahydrofolate deformylase
IPR005794 Methionyl-tRNA formyltransferase
IPR009188 [NiFe]-hydrogenase maturation factor, HypX/HoxX type
IPR011407 10-formyltetrahydrofolate dehydrogenase
IPR015518 Methionine tRNA Formyltransferase-like

Contains

IPR001555 Phosphoribosylglycinamide formyltransferase, active site

GO Term annotation Help

Process

GO:0009058 biosynthetic process

Function

GO:0016742 hydroxymethyl-, formyl- and related transferase activity

InterPro annotation

Entry Details in BioMart

Abstract

A number of formyl transferases belong to this group. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. Formyltetrahydrofolate dehydrogenase produces formate from formyl- tetrahydrofolate. This is the N-terminal domain of these enzymes and is found upstream of the C-terminal domain (IPR005793).

The trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase catalyses the second, third and fifth steps in de novo purine biosynthesis. The glycinamide ribonucleotide transformylase belongs to this group.

Structural links Help

PDB - click here

SCOP: c.65.1.1

CATH: 3.40.50.170

Database links Help

Enzyme: EC:2.1.2.9

PANDIT: PF00551

Blocks: IPB002376

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002376

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O75891 10-formyltetrahydrofolate dehydrogenase

P00967 Trifunctional purine biosynthetic protein adenosine-3

P04161 Phosphoribosylglycinamide formyltransferase

P52422 Phosphoribosylglycinamide formyltransferase, chloroplastic

Q64737 Trifunctional purine biosynthetic protein adenosine-3

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002376	Formyl transferase, N-terminal
IPR011761	ATP-grasp fold
IPR001555	Phosphoribosylglycinamide formyltransferase, active site
IPR011034	Formyl transferase, C-terminal-like
IPR010918	AIR synthase related protein, C-terminal
IPR004733	Phosphoribosylformylglycinamidine cyclo-ligase
IPR011054	Rudiment single hybrid motif
IPR020561	Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain
IPR020560	Phosphoribosylglycinamide synthetase, C-domain
IPR009081	Acyl carrier protein-like
IPR020562	Phosphoribosylglycinamide synthetase, N-domain
IPR000115	Phosphoribosylglycinamide synthetase
IPR011407	10-formyltetrahydrofolate dehydrogenase
IPR013815	ATP-grasp fold, subdomain 1
IPR013816	ATP-grasp fold, subdomain 2
IPR013817	Pre-ATP-grasp fold
IPR020559	Phosphoribosylglycinamide synthetase, conserved site
IPR004607	Phosphoribosylglycinamide formyltransferase
IPR005793	Formyl transferase, C-terminal
IPR016188	PurM, N-terminal-like
IPR016162	Aldehyde dehydrogenase, N-terminal
IPR016161	Aldehyde/histidinol dehydrogenase
IPR016160	Aldehyde dehydrogenase, conserved site
IPR016185	PreATP-grasp-like fold
IPR015590	Aldehyde dehydrogenase
IPR000728	AIR synthase related protein
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Dahms TE, Sainz G, Giroux EL, Caperelli CA, Smith JL. The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase. Biochemistry 44 2005 9841-50 [PubMed: 16026156] http://dx.doi.org/10.1021/bi050307g
	Gatzeva-Topalova PZ, May AP, Sousa MC. Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance. Biochemistry 44 2005 5328-38 [PubMed: 15807526] http://dx.doi.org/10.1021/bi047384g
	Kursula P, Schuler H, Flodin S, Nilsson-Ehle P, Ogg DJ, Savitsky P, Nordlund P, Stenmark P. Structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue. Acta Crystallogr. D Biol. Crystallogr. 62 2006 1294-9 [PubMed: 17057331] http://dx.doi.org/10.1107/S0907444906026849
	Gatzeva-Topalova PZ, May AP, Sousa MC. Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance. Structure 13 2005 929-42 [PubMed: 15939024] http://dx.doi.org/10.1016/j.str.2005.03.018
	Williams GJ, Breazeale SD, Raetz CR, Naismith JH. Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis. J. Biol. Chem. 280 2005 23000-8 [PubMed: 15809294] http://dx.doi.org/10.1074/jbc.M501534200
	Chen P, Schulze-Gahmen U, Stura EA, Inglese J, Johnson DL, Marolewski A, Benkovic SJ, Wilson IA. Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 A resolution. A target enzyme for chemotherapy. J. Mol. Biol. 227 1992 283-92 [PubMed: 1522592] http://dx.doi.org/10.1016/0022-2836(92)90698-J

InterPro 23.1