AT5G57030.1 :

DomainDescriptionEvalueBitsGAStartEnd
Thi4Thi4 family4.4E-051220.00109169
FAD_oxidoredFAD dependent oxidoreductase4.2E-051227.00110139
Lycopene_cyclLycopene cyclase protein053223.40110501
Pyr_redox_2Pyridine nucleotide-disulphide oxidoreductase2.3E-072022.80110144
DAOFAD dependent oxidoreductase0.000231024.70110140
HI0933_likeHI0933-like protein1.7E-051320.30110137
GIDAGlucose inhibited division protein A3E-061620.00110144
FAD_binding_2FAD binding domain1.2E-051420.40110136
Pyr_redox_3Pyridine nucleotide-disulphide oxidoreductase0.000231030.00112134
DAOFAD dependent oxidoreductase0.0023724.70188277
Pyr_redox_2Pyridine nucleotide-disulphide oxidoreductase0.044222.80195249
HI0933_likeHI0933-like protein0.016320.30196248
T3SS_LEE_assocType III secretion system subunit0.000111225.00400453

 524

Thi4
FAD_oxidored
Lycopene_cycl
Pyr_redox_2
DAO
HI0933_like
GIDA
FAD_binding_2
Pyr_redox_3
DAO
Pyr_redox_2
HI0933_like
T3SS_LEE_assoc


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.

HI0933_like

T3SS_LEE_assoc

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

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.

GIDA

FAD_oxidored

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.

Pyr_redox_3

Thi4
7961415 Cloning, nucleotide sequence, and regulation of Schizosaccharomyces pombe thi4, a thiamine biosynthetic gene. J Bacteriol 1994;176:6631-6635.