264109 fabG
Thalassiosira pseudonana

Chromosome Product Transcript Start End Strand Short Name
264109 chr_14 fabG 131108 132365 - fabG
Expression Profile Conditional Changes Cluster Dendrogram
Thaps_hclust_0101
Normalized Mean Residue
Thaps_bicluster_0051
0.39
hypothetical protein
0.9217
0.9216
Zip superfamily
0.9151
hypothetical protein
0.9124
hypothetical protein
0.9082
GRX_PICOT_like
0.9047
TRX_family
0.9046
PRK05279
0.9044
hypothetical protein
0.9004
Cyt_c_Oxidase_VIb
0.8988
Name CD Accession Definition Superfamily Bitscore E-Value From - To Hit Type PSSM ID
SDR_c classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single... cl09931 206.366 1.17E-65 12 - 260 specific 212491
NADB_Rossmann superfamily Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD... - 206.366 1.17E-65 12 - 260 superfamily 263925
fabG 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional - 211.227 2.72E-67 5 - 261 multi-dom 235975
T. pseudonana P. tricornutum P. tricornutum DiatomCyc F. cylindrus Pseudo-nitzschia multiseries E. huxleyi C. reinhardtii A. thaliana P. sojae
Not available PHATR_25739 PHATR_25739 277428 309172 Not available Not available AT3G46170.1 Not available
KEGG description KEGG Pathway
Not available Not available
GO:0008152 GO:0016491 -

metabolic process

Details: 
The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
GO Category: 
BP

oxidoreductase activity

Details: 
Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO Category: 
MF
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