AT1G72970.1 :

DomainDescriptionEvalueBitsGAStartEnd
GMC_oxred_NGMC oxidoreductase3.5E-3210120.5063335
Pyr_redox_2Pyridine nucleotide-disulphide oxidoreductase1.3E-051322.806395
DAOFAD dependent oxidoreductase2.4E-061624.706496
Lycopene_cyclLycopene cyclase protein3.7E-061523.4064102
FAD_binding_2FAD binding domain2.7E-071920.4064298
NAD_binding_8NAD(P)-binding Rossmann-like domain3.1E-061621.906796
GMC_oxred_CGMC oxidoreductase5.5E-309421.00431577

 594

GMC_oxred_N
Pyr_redox_2
DAO
Lycopene_cycl
FAD_binding_2
NAD_binding_8
GMC_oxred_C


References:

Lycopene_cycl
8837512 Functional analysis of the beta and epsilon lycopene cyclase enzymes of Arabidopsis reveals a mechanism for control of cyclic carotenoid formation. Plant Cell 1996;8:1613-1626.
11226339 One ring or two? Determination of ring number in carotenoids by lycopene epsilon-cyclases. Proc Natl Acad Sci U S A 2001;98:2905-2910.

DAO
9153426 Active site plasticity in D-amino acid oxidase: a crystallographic analysis. Biochemistry 1997;36:5853-5860.

GMC_oxred_N

GMC_oxred_C

FAD_binding_2
8061609 Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Protein Sci 1994;3:799-809.

NAD_binding_8

Pyr_redox_2
8805537 Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Structure 1996;4:277-286.