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InterPro: IPR004607 Phosphoribosylglycinamide formyltransferase

Protein matchesHelp
UniProtKB
Matches:
1633 proteins
AccessionHelp IPR004607 PurN_trans
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR001555 Phosphoribosylglycinamide formyltransferase, active site
IPR002376 Formyl transferase, N-terminal
GO Term annotationHelp
Process GO:0006189 'de novo' IMP biosynthetic process
Function GO:0004644 phosphoribosylglycinamide formyltransferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This family describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins found in formyltransferase. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of Escherichia coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis thaliana. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup.

Structural linksHelp
SCOP: c.65.1.1
CATH: 3.40.50.170
Database linksHelp
Enzyme: EC:2.1.2.2

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR004607 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P00967 Trifunctional purine biosynthetic protein adenosine-3

P04161 Phosphoribosylglycinamide formyltransferase

P22102 Trifunctional purine biosynthetic protein adenosine-3

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
IPR013815 ATP-grasp fold, subdomain 1
IPR013816 ATP-grasp fold, subdomain 2
IPR002376 Formyl transferase, N-terminal
IPR013817 Pre-ATP-grasp fold
IPR020559 Phosphoribosylglycinamide synthetase, conserved site
IPR004607 Phosphoribosylglycinamide formyltransferase
IPR016188 PurM, N-terminal-like
IPR016185 PreATP-grasp-like fold
IPR011761 ATP-grasp fold
IPR001555 Phosphoribosylglycinamide formyltransferase, active site
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
IPR020562 Phosphoribosylglycinamide synthetase, N-domain
IPR000728 AIR synthase related protein
IPR000115 Phosphoribosylglycinamide synthetase
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp

Additional ReadingHelp
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
Greasley SE, Marsilje TH, Cai H, Baker S, Benkovic SJ, Boger DL, Wilson IA.
Unexpected formation of an epoxide-derived multisubstrate adduct inhibitor on the active site of GAR transformylase.
Biochemistry 40 2001 13538-47 [PubMed: 11695901]
http://dx.doi.org/10.1021/bi011482+
Smith JM, Daum HA 3rd.
Identification and nucleotide sequence of a gene encoding 5'-phosphoribosylglycinamide transformylase in Escherichia coli K12.
J. Biol. Chem. 262 1987 10565-9 [PubMed: 3301838]
http://intl.jbc.org/cgi/reprint/262/22/10565.pdf
Zhang Y, Desharnais J, Greasley SE, Beardsley GP, Boger DL, Wilson IA.
Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR.
Biochemistry 41 2002 14206-15 [PubMed: 12450384]
http://dx.doi.org/10.1021/bi020522m
Zhang Y, Desharnais J, Marsilje TH, Li C, Hedrick MP, Gooljarsingh LT, Tavassoli A, Benkovic SJ, Olson AJ, Boger DL, Wilson IA.
Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid.
Biochemistry 42 2003 6043-56 [PubMed: 12755606]
http://dx.doi.org/10.1021/bi034219c
Greasley SE, Yamashita MM, Cai H, Benkovic SJ, Boger DL, Wilson IA.
New insights into inhibitor design from the crystal structure and NMR studies of Escherichia coli GAR transformylase in complex with beta-GAR and 10-formyl-5,8,10-trideazafolic acid.
Biochemistry 38 1999 16783-93 [PubMed: 10606510]
http://dx.doi.org/10.1021/bi991888a
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InterPro 23.1