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InterPro: IPR013982 AICARFT/IMPCHase bienzyme, transformylase domain

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UniProtKB

Matches:

1901 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
Matches in BioMart

Accession

IPR013982 AICARFT_IMPCHase_bienz

Secondary

IPR002695

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01808	AICARFT_IMPCHas	1887
SMART	SM00798	AICARFT_IMPCHas	1840
SuperFamily	SSF64197	AICARFT_IMPCHas_formly	1855
Signatures in BioMart

InterPro Relationships Help

Found in

IPR002695 AICARFT/IMPCHase bienzyme

GO Term annotation Help

Process

GO:0006188 IMP biosynthetic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a region associated with formylation activity which is found in a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate [1]. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP [1].

Structural links Help

PDB - click here

SCOP: c.24.1.3 , c.97.1.4

CATH: 1.10.287.440 , 3.40.140.20 , 3.40.50.1380

Database links Help

Enzyme: EC:2.1.2.3 , EC:3.5.4.10

Pfam Clan: CL0109.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013982

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P31939 Bifunctional purine biosynthesis protein PURH

P38009 Bifunctional purine biosynthesis protein ADE17

P74741 Bifunctional purine biosynthesis protein purH

Q9CWJ9 Bifunctional purine biosynthesis protein PURH

Q9X0X6 Bifunctional purine biosynthesis protein purH

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002695	AICARFT/IMPCHase bienzyme
IPR011607	MGS-like
IPR013982	AICARFT/IMPCHase bienzyme, transformylase domain
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Akira T, Komatsu M, Nango R, Tomooka A, Konaka K, Yamauchi M, Kitamura Y, Nomura S, Tsukamoto I. Molecular cloning and expression of a rat cDNA encoding 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Gene 197 289-93 1997 [PubMed: 9332377] http://dx.doi.org/10.1016/S0378-1119(97)00273-4

Additional Reading Open in usermanual
	Xu L, Li C, Olson AJ, Wilson IA. Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide transformylase in complex with a novel non-folate inhibitor identified by virtual ligand screening. J. Biol. Chem. 279 2004 50555-65 [PubMed: 15355974] http://dx.doi.org/10.1074/jbc.M406801200
	Rayl EA, Moroson BA, Beardsley GP. The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping. J. Biol. Chem. 271 1996 2225-33 [PubMed: 8567683] http://dx.doi.org/10.1074/jbc.271.4.2225
	Axelrod HL, McMullan D, Krishna SS, Miller MD, Elsliger MA, Abdubek P, Ambing E, Astakhova T, Carlton D, Chiu HJ, Clayton T, Duan L, Feuerhelm J, Grzechnik SK, Hale J, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Quijano K, Reyes R, Rife CL, van den Bedem H, Weekes D, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA. Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 A resolution. Proteins 71 2008 1042-9 [PubMed: 18260100] http://dx.doi.org/10.1002/prot.21967
	Wolan DW, Greasley SE, Wall MJ, Benkovic SJ, Wilson IA. Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor beta-DADF identifies the folate binding site. Biochemistry 42 2003 10904-14 [PubMed: 12974624] http://dx.doi.org/10.1021/bi030106h
	Wolan DW, Cheong CG, Greasley SE, Wilson IA. Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor. Biochemistry 43 2004 1171-83 [PubMed: 14756553] http://dx.doi.org/10.1021/bi030162i
	Cheong CG, Wolan DW, Greasley SE, Horton PA, Beardsley GP, Wilson IA. Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates. J. Biol. Chem. 279 2004 18034-45 [PubMed: 14966129] http://dx.doi.org/10.1074/jbc.M313691200

InterPro 23.1