EC number:2.7.4.31

Enzyme

Download
EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.4 Phosphotransferases with a phosphate group as acceptor
ID:2.7.4.31
Description:(5-(aminomethyl)furan-3-yl)methyl phosphate kinase.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.4.31
BRENDA Enzyme Link: BRENDA 2.7.4.31
KEGG Enzyme Link: KEGG2.7.4.31
BioCyc Enzyme Link: BioCyc 2.7.4.31
ExPASy Enzyme Link: ExPASy2.7.4.31
EC2PDB Enzyme Link: EC2PDB 2.7.4.31
ExplorEnz Enzyme Link: ExplorEnz 2.7.4.31
PRIAM enzyme-specific profiles Link: PRIAM 2.7.4.31
IntEnz Enzyme Link: IntEnz 2.7.4.31
MEDLINE Enzyme Link: MEDLINE 2.7.4.31

EC number:2.7.4.31

MSA:

2.7.4.31;
Phylogenetic Tree:

2.7.4.31;
Uniprot:
M-CSA:
RHEA:47836 [5-(aminomethyl)-3-furyl]methyl phosphate + ATP = [5-(aminomethyl)furan-3-yl]methyl diphosphate + ADP
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification of the Final Two Genes Functioning in Methanofuran Biosynthesis in Methanocaldococcus jannaschii.Wang Y, Xu H, Jones MK, White RH2015 Sep26100040