AT1G73050.1 :

DomainDescriptionEvalueBitsGAStartEnd
GMC_oxred_NGMC oxidoreductase1.6E-3210220.5054325
Pyr_redox_2Pyridine nucleotide-disulphide oxidoreductase4.9E-071822.805493
DAOFAD dependent oxidoreductase8.4E-061524.705584
Lycopene_cyclLycopene cyclase protein2E-051323.405585
FAD_binding_3FAD binding domain0.000121020.105589
Pyr_redox_3Pyridine nucleotide-disulphide oxidoreductase3.1E-051230.0057124
NAD_binding_8NAD(P)-binding Rossmann-like domain2.6E-061721.905884
GMC_oxred_CGMC oxidoreductase4.1E-288821.00399540

 552

GMC_oxred_N
Pyr_redox_2
DAO
Lycopene_cycl
FAD_binding_3
Pyr_redox_3
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

FAD_binding_3
1409567 Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3A resolution. Proteins 1992;14:178-190.

NAD_binding_8

Pyr_redox_3

GMC_oxred_C

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.