_EC 2.7.7.2 Fad synthetase. 10 PDB entries  
EC 2.-.-.- Transferases. [17,943 PDB entries]
EC 2.7.-.- Transferring phosphorous-containing groups. [10,910 PDB entries]
EC 2.7.7.- Nucleotidyltransferases. [4,486 PDB entries]
EC 2.7.7.2 Fad synthetase. [10 PDB entries]    
1mrz

Reaction: Atp + fmn = diphosphate + fad.
 


ATP
+
FMN
=
diphosphate
+
FAD
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Fad diphosphorylase. Fad pyrophosphorylase. Fads. Flavin adenine dinucleotide synthetase. Fmn adenylyltransferase.
Cofactor(s): Mg(2+).
Comments: Highly specific for Atp as phosphate donor. The cofactors Fmn and fad participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates. While monofunctional Fad synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of Ec 2.7.1.26.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 10 PDB entries in enzyme class E.C.2.7.7.2

  PDB code Protein
1mrz
Crystal structure of a flavin binding protein from thermotog maritima, tm379
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm379. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (266 residues) CATH domains: 3.40.50.620 2.40.30.30
1s4m
Crystal structure of flavin binding to fad synthetase from thermotoga maritina
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (277 residues) CATH domains: 3.40.50.620 2.40.30.30
1t6x
Crystal structure of adp bound tm379
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (266 residues) CATH domains: 3.40.50.620 2.40.30.30
1t6y
Crystal structure of adp, amp, and fmn bound tm379
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (268 residues) CATH domains: 3.40.50.620 2.40.30.30
1t6z
Crystal structure of riboflavin bound tm379
Source: Thermotoga maritima. Organism_taxid: 2336. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (266 residues) CATH domains: 3.40.50.620 2.40.30.30
2i1l
Crystal structure of the c2 form of fad synthetase from thermotoga maritima
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm_0857. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (267 residues) CATH domains: 3.40.50.620 2.40.30.30
2wsi
Crystal structure of yeast fad synthetase (fad1) in complex with fad
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (285 residues)
Bound ligand:   Het Group FAD corresponds to enzyme product FAD
2x0k
Crystal structure of modular fad synthetase from corynebacterium ammoniagenes
Source: Corynebacterium ammoniagenes. Organism_taxid: 1697. Atcc: 6872. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (338 residues) CATH domains: 3.40.50.620 2.40.30.30
Bound ligand:   Het Group PPV corresponds to enzyme product diphosphate
3glv
Crystal structure of the lipopolysaccharide core biosynthesi from thermoplasma volcanium gss1
Source: Thermoplasma volcanium gss1. Organism_taxid: 273116. Strain: gss1 / dsm 4299 / ifo 15438 / jcm 9571. Atcc: 51530. Gene: gi:14325477, tv1239, tvg1279046. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (122 residues) CATH domain: 3.40.50.620
Bound ligand:   Het Group AMP is 74.19% similar to enzyme reactant ATP
3zug
E268d mutant of fad synthetase from corynebacterium ammoniag
Source: Corynebacterium ammoniagenes. Organism_taxid: 1697. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (335 residues) CATH domains: 3.40.50.620 2.40.30.30