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Links from Protein

Items: 6

1.

MGS-like domain

This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site [1]. [1]. 10526357. Structure classification-based assessment of CASP3 predictions. for the fold recognition targets.. Murzin AG;. Proteins 1999;37:88-103. (from Pfam)

Date:
2024-08-14
Family Accession:
NF014225.5
Method:
HMM
2.

AICARFT/IMPCHase bienzyme

This is 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]. This is catalysed by a pair of C-terminal deaminase fold domains in the protein [3], where the active site is formed by the dimeric interface of two monomeric units [3]. The last step is catalysed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP [1]. [1]. 9332377. Molecular cloning and expression of a rat cDNA encoding 5-. aminoimidazole-4-carboxamide ribonucleotide. formyltransferase/IMP cyclohydrolase [published erratum appears. in Gene 1998 Feb 27;208(2):337]. Akira T, Komatsu M, Nango R, Tomooka A, Konaka K, Yamauchi M,. Kitamura Y, Nomura S, Tsukamoto I;. Gene 1997;197:289-293.. [2]. 8567683. The human purH gene product, 5-aminoimidazole-4-carboxamide. ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning,. sequencing, expression, purification, kinetic analysis, and. domain mapping.. Rayl EA, Moroson BA, Beardsley GP;. J Biol Chem 1996;271:2225-2233.. [3]. 21890906. Evolution of the deaminase fold and multiple origins of. eukaryotic editing and mutagenic nucleic acid deaminases from. bacterial toxin systems.. Iyer LM, Zhang D, Rogozin IB, Aravind L;. Nucleic Acids Res. 2011; [Epub . TRUNCATED at 1650 bytes (from Pfam)

GO Terms:
Molecular Function:
IMP cyclohydrolase activity (GO:0003937)
Molecular Function:
phosphoribosylaminoimidazolecarboxamide formyltransferase activity (GO:0004643)
Biological Process:
purine nucleotide biosynthetic process (GO:0006164)
Date:
2024-08-14
Family Accession:
NF013931.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.

bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase

Gene:
purH
GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Molecular Function:
IMP cyclohydrolase activity (GO:0003937)
Molecular Function:
phosphoribosylaminoimidazolecarboxamide formyltransferase activity (GO:0004643)
Biological Process:
purine nucleotide biosynthetic process (GO:0006164)
Biological Process:
'de novo' IMP biosynthetic process (GO:0006189)
Date:
2021-07-21
Family Accession:
NF002049.0
Method:
HMM
6.

bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase

PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region.

Gene:
purH
GO Terms:
Molecular Function:
IMP cyclohydrolase activity (GO:0003937)
Molecular Function:
phosphoribosylaminoimidazolecarboxamide formyltransferase activity (GO:0004643)
Biological Process:
purine ribonucleotide biosynthetic process (GO:0009152)
Date:
2021-04-27
Family Accession:
TIGR00355.1
Method:
HMM
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