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Assembly Name: biogeco3 v1.0

Name: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors

Term: GO:0016706  Help

Source: GO from Blast2go

Ontology: Molecular Function

UniGenes with this annotation:

Sequence Assembly Length (nt)
DescriptionE-value
 Full-Length
biog3_v1.0_unigene409 biogeco3 v1.0 345
• AutoFact: Hyoscyamine 6-dioxygenase, putative n=1 Tax=Ricinus communis RepID=B9RKI5_RICCO 5.0e-30
• FL-Next: tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis). 0.0
• Blast2go: 2-oxoglutarate and fe -dependent oxygenase-like protein 7.64157e-36
N-terminus
biog3_v1.0_unigene3315 biogeco3 v1.0 717
• AutoFact: oxidoreductase, 2OG-Fe(II) oxygenase family protein [Arabidopsis thaliana] gb|AAD03425.1| contains similarity to Iron/Ascorbate family of oxidoreductases (Pfam: PF00671, Score=297.8, E=1.3e-85, N=1) [Arabidopsis thaliana] emb|CAB40043.1| putative Fe(II)/a 0.0
• FL-Next: tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis). 0.0
• Blast2go: 2og-fe oxygenase family protein 0.0
C-terminus
biog3_v1.0_unigene7268 biogeco3 v1.0 913
• AutoFact: oxidoreductase, 2OG-Fe(II) oxygenase family protein [Arabidopsis thaliana] gb|AAD03425.1| contains similarity to Iron/Ascorbate family of oxidoreductases (Pfam: PF00671, Score=297.8, E=1.3e-85, N=1) [Arabidopsis thaliana] emb|CAB40043.1| putative Fe(II)/a 0.0
• FL-Next: tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis). 0.0
• Blast2go: 2og-fe oxygenase family protein 0.0
C-terminus
biog3_v1.0_unigene13704 biogeco3 v1.0 434
• AutoFact: 2-oxoacid-dependent dioxygenase n=2 Tax=Selaginella moellendorffii RepID=D8R3W5_SELML 0.0
• FL-Next: tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis). 0.0
• Blast2go: 2-oxoacid-dependent dioxygenase 0.0
Internal

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Biología Molecular y Biotecnología de Plantas, Facultad de Ciencias y Plataforma Andaluza de Bioinformática, Universidad de Málaga, E-29071 Málaga, Spain