EC number:4.3.1.4

Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.1 Ammonia-lyases
ID:4.3.1.4
Description:Formimidoyltetrahydrofolate cyclodeaminase.
Alternative Name: Formiminotetrahydrofolate cyclodeaminase.
Cath: 1.20.120.680; 3.30.70.670; 3.30.990.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.1.4
BRENDA Enzyme Link: BRENDA 4.3.1.4
KEGG Enzyme Link: KEGG4.3.1.4
BioCyc Enzyme Link: BioCyc 4.3.1.4
ExPASy Enzyme Link: ExPASy4.3.1.4
EC2PDB Enzyme Link: EC2PDB 4.3.1.4
ExplorEnz Enzyme Link: ExplorEnz 4.3.1.4
PRIAM enzyme-specific profiles Link: PRIAM 4.3.1.4
IntEnz Enzyme Link: IntEnz 4.3.1.4
MEDLINE Enzyme Link: MEDLINE 4.3.1.4

EC number:4.3.1.4

MSA:

4.3.1.4;
Phylogenetic Tree:

4.3.1.4;
Uniprot:
M-CSA:
RHEA:22736 5-formimidoyltetrahydrofolate + 2 H(+) = 5,10-methenyltetrahydrofolate + NH4(+)
RULE(radius=1) [*:1]-[NH;+0:2]-[*:3]-[*:4]-[N;H0;+0:5](-[*:6])-[CH;+0:7]=[NH;+0:8].[H+;H0:9].[H+;H0:10]>>[*:1]-[N;H0;+0:2]1-[*:3]-[*:4]-[N+;H0:5](-[*:6])=[CH;+0:7]-1.[NH3;+0:8]
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References

TitleAuthorsDatePubMed ID
Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer.Mao Y, Vyas NK, Vyas MN, Chen DH, Ludtke SJ, Chiu W, Quiocho FA2004 Aug 415272307
The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A2000 Jan 1510673422