AT3G10230.1 :

DomainDescriptionEvalueBitsGAStartEnd
Thi4Thi4 family1.7E-051420.0079112
K_oxygenaseL-lysine 6-monooxygenase (NADPH-requiring)0.000361021.0081120
FAD_binding_3FAD binding domain1.3E-061820.1083112
GIDAGlucose inhibited division protein A0.00054920.0084109
FAD_binding_2FAD binding domain8.5E-061520.4084112
Lycopene_cyclLycopene cyclase protein050623.4084478
Pyr_redox_2Pyridine nucleotide-disulphide oxidoreductase4.6E-061622.8084112
DAOFAD dependent oxidoreductase1.7E-051524.7084114
FAD_oxidoredFAD dependent oxidoreductase2.9E-061727.0084223
HI0933_likeHI0933-like protein4.4E-061620.3084116
Pyr_redoxPyridine nucleotide-disulphide oxidoreductase0.00041122.0085118
Trp_halogenaseTryptophan halogenase0.0088519.6085105
XdhC_CXdhC Rossmann domain0.000171229.7085126
NAD_binding_9FAD-NAD(P)-binding0.000781021.8086104
Pyr_redox_3Pyridine nucleotide-disulphide oxidoreductase3.2E-051330.0087108
NAD_binding_8NAD(P)-binding Rossmann-like domain1.5E-051521.9087114
Pyr_redox_2Pyridine nucleotide-disulphide oxidoreductase1.3E-051522.80158222
DAOFAD dependent oxidoreductase9.8E-061524.70161258
Trp_halogenaseTryptophan halogenase3.6E-051319.60165227
GIDAGlucose inhibited division protein A0.0027720.00165221
Pyr_redoxPyridine nucleotide-disulphide oxidoreductase0.1322.00169204
HI0933_likeHI0933-like protein0.089220.30171220
NAD_binding_9FAD-NAD(P)-binding0.000281121.80180220
Pyr_redox_3Pyridine nucleotide-disulphide oxidoreductase0.0026730.00187238
FAD_binding_2FAD binding domain0.84-120.40187223
Thi4Thi4 family0.0046620.00192223
Pyr_redoxPyridine nucleotide-disulphide oxidoreductase0.54122.00309327

 501

Thi4
K_oxygenase
FAD_binding_3
GIDA
FAD_binding_2
Lycopene_cycl
Pyr_redox_2
DAO
FAD_oxidored
HI0933_like
Pyr_redox
Trp_halogenase
XdhC_C
NAD_binding_9
Pyr_redox_3
NAD_binding_8
Pyr_redox_2
DAO
Trp_halogenase
GIDA
Pyr_redox
HI0933_like
NAD_binding_9
Pyr_redox_3
FAD_binding_2
Thi4
Pyr_redox


References:

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.

XdhC_C

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.

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

HI0933_like

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

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
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.

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

GIDA

Pyr_redox_3

FAD_oxidored

K_oxygenase

Trp_halogenase
10547442 Conservation of the pyrrolnitrin biosynthetic gene cluster among six pyrrolnitrin-producing strains. FEMS Microbiol Lett 1999;180:39-44.

NAD_binding_9

NAD_binding_8