|
||||||
|
UniGene Name: sp_v3.0_unigene119026
Length: 245 nt
 UniGene Fasta
|
|---|
| >sp_v3.0_unigene119026
A |
|
Ace file of the UniGene sp_v3.0_unigene119026
|
|---|
If you push the Download ace button, you will download an ace file of this UniGene.
To watch this ACE file you will need an ACE viewer program as Tablet:
Go to the Tablet ACE viewer Web
| Annotations |
|---|
| Source | Descriptions | Term | Type | e value | Identity |
|---|---|---|---|---|---|
| AutoFact | Dihydrolipoamide acetyltransferase n=1 Tax=Laccaria bicolor S238N-H82 RepID=B0CQH3_LACBS | - | - | 1.0e-27 | 76% |
| FL-Next | tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis). | - | - | 0.0 | 46% |
| Source | ECs | Term | Type | e value | Identity |
|---|---|---|---|---|---|
| Sma3 | Dihydrolipoyllysine-residue acetyltransferase. | EC:2.3.1.12 | - | 2.898e-07 | - |
| Source | KEGGs | Term | Type | e value | Identity |
|---|---|---|---|---|---|
| Sma3 | Glycolysis / Gluconeogenesis | 00010 | 2.898e-07 | % | |
| Sma3 | Citrate cycle (TCA cycle) | 00020 | 2.898e-07 | % | |
| Sma3 | Pyruvate metabolism | 00620 | 2.898e-07 | % | |
| Sma3 | Biosynthesis of phenylpropanoids | 01061 | 2.898e-07 | % | |
| Sma3 | Biosynthesis of terpenoids and steroids | 01062 | 2.898e-07 | % | |
| Sma3 | Biosynthesis of alkaloids derived from shikimate pathway | 01063 | 2.898e-07 | % | |
| Sma3 | Biosynthesis of alkaloids derived from ornithine, lysine and nicotinic acid | 01064 | 2.898e-07 | % | |
| Sma3 | Biosynthesis of alkaloids derived from histidine and purine | 01065 | 2.898e-07 | % | |
| Sma3 | Biosynthesis of alkaloids derived from terpenoid and polyketide | 01066 | 2.898e-07 | % | |
| Sma3 | Biosynthesis of plant hormones | 01070 | 2.898e-07 | % | |
| Sma3 | Metabolic pathways | 01100 | 2.898e-07 | % | |
| Sma3 | Biosynthesis of secondary metabolites | 01110 | 2.898e-07 | % |
| Source | Gene names |
|---|---|
| Sma3 | CHLREDRAFT_149709; DLA1; MICPUCDRAFT_25687; MICPUN_96637; OSTLU_31760; OSTLU_4381; Ot05g03030; |
| Source | GOs | Term | Type | e value | Identity |
|---|---|---|---|---|---|
| Sma3 | pyruvate dehydrogenase complex | GO:0045254 | Cellular Component | 0.0 | - |
| Sma3 | dihydrolipoyllysine-residue acetyltransferase activity | GO:0004742 | Molecular Function | 0.0 | - |
| Sma3 | protein binding | GO:0005515 | Molecular Function | 0.0 | - |
| Sma3 | GO:0008415 | Molecular Function | 0.0 | - | |
| Sma3 | pyruvate metabolic process | GO:0006090 | Biological Process | 0.0 | - |
| Sma3 | metabolic process | GO:0008152 | Biological Process | 0.0 | - |
| Source | InterPros | Term | Type | e value | Identity |
|---|---|---|---|---|---|
| Sma3 | Biotin/lipoyl attachment | IPR000089 | - | 0.0 | - |
| Sma3 | 2-oxoacid dehydrogenase acyltransferase, catalytic domain | IPR001078 | - | 0.0 | - |
| Sma3 | 2-oxo acid dehydrogenase, lipoyl-binding site | IPR003016 | - | 0.0 | - |
| Sma3 | E3 binding | IPR004167 | - | 0.0 | - |
| Sma3 | Dihydrolipoamide acetyltransferase, long form | IPR006257 | - | 0.0 | - |
| Source | Species | ID | Description | e value | Identity |
|---|---|---|---|---|---|
| ATG | Arabidoptis thaliana | AT1G54220.1 | Dihydrolipoamide acetyltransferase, long form protein chr1:20246460-20250208 REVERSE LENGTH=539 | 1.0e-21 | 50% |
| RefSeq | Arabidopsis thaliana | NP_564654.1 | dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex [Arabidopsis thaliana] | 2.0e-21 | 50% |
| RefSeq | Populus trichocarpa | XP_002303212.1 | predicted protein [Populus trichocarpa] | 2.0e-19 | 45% |
| Full-Lengther Next Prediction |
|---|
Fln status: Internal
Fln database: coniferopsida.fasta
Fln subject: B8LLY8
Fln msg: Distance to subject end: 98 aas, your sequence is shorter than subject: 81 - 566
Fln protein:
K
Protein Length:
82
Fln nts:
A
Fln Alignment:
AllPine_a_c54404___GAKLSVNDFIVKAVGLALADVPEANTSWMGDYIRQWKKADVSIAVATPTGLITPIVTDIGSKGLTTISAEAKALAKKARD
B8LLY8________________GKRISVNDFVIKAAASALRKVPQCNSSWTNEYIRQYHNINISVAVQTDKGLFVPVVKDADKKGLSAIGEDVKVLAQKAKE
Biología Molecular y Biotecnología de Plantas, Facultad de Ciencias y Plataforma Andaluza de Bioinformática, Universidad de Málaga, E-29071 Málaga, Spain
