32431 Fe_bilin_red superfamily
Thalassiosira pseudonana

Chromosome Product Transcript Start End Strand Short Name
32431 chr_2 Fe_bilin_red superfamily 2070412 2071665 + Fe_bilin_red superfamily
NCBI ID Ensembl Genomes exon ID
7452353 Thaps32431.1
Expression Profile Conditional Changes Cluster Dendrogram
Thaps_hclust_0024
Normalized Mean Residue
Thaps_bicluster_0129
0.19
PLN00015
0.9384
hypothetical protein
0.9325
hypothetical protein
0.9316
NAD_binding_8 superfamily
0.9308
Cob-chelat-sub
0.9297
Chloroa_b-bind
0.9287
(bd1342) psaL
0.9281
(bd2088) rbcL
0.9279
(bd1403) NA
0.9276
MviM
0.9274
Name CD Accession Definition Superfamily Bitscore E-Value From - To Hit Type PSSM ID
Fe_bilin_red superfamily Ferredoxin-dependent bilin reductase; This family consists of several different but closely related... - 201.782 7.13E-62 153 - 360 superfamily 263512
T. pseudonana P. tricornutum P. tricornutum DiatomCyc F. cylindrus Pseudo-nitzschia multiseries E. huxleyi C. reinhardtii A. thaliana P. sojae
Not available PHATRDRAFT_10830 PHATRDRAFT_10830 181161 299095 Not available Not available Not available Not available
KEGG description KEGG Pathway
Not available Not available
GO:0010024 GO:0016636 GO:0050897 GO:0050619 -

phytochromobilin biosynthetic process

Details: 
The chemical reactions and pathways resulting in the formation of phytochromobilin, which involves the oxidative cleavage of heme by a heme oxygenase(HO) to form biliverdin IX alpha.
GO Category: 
BP

oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor

Details: 
Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces an iron-sulfur protein.
GO Category: 
MF

cobalt ion binding

Details: 
Interacting selectively and non-covalently with a cobalt (Co) ion.
GO Category: 
MF

phytochromobilin:ferredoxin oxidoreductase activity

Details: 
Catalysis of the reaction: (3Z)-phytochromobilin + oxidized ferredoxin = biliverdin IXa + reduced ferredoxin.
GO Category: 
MF
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