UniGene Name: sp_v3.0_unigene208028
Length: 240 nt
This UniGene was originaly assembled in antisense
ACE File: antisense
Fasta: sense
UniGene Fasta (sense) |
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>sp_v3.0_unigene208028
G |
Ace file of the UniGene sp_v3.0_unigene208028 (antisense) |
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Annotations |
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Source | Descriptions | Term | Type | e value | Identity |
---|---|---|---|---|---|
AutoFact | Acetohydroxyacid isomeroreductase n=1 Tax=Glycine max RepID=D2DKE6_SOYBN | - | - | 3.0e-23 | 75% |
FL-Next | tr=Putative uncharacterized protein; Picea sitchensis (Sitka spruce) (Pinus sitchensis). | - | - | 0.0 | 91% |
Sma3 | Ketol-acid reductoisomerase | - | - | 1.611e-14 | - |
Source | ECs | Term | Type | e value | Identity |
---|---|---|---|---|---|
Sma3 | Ketol-acid reductoisomerase. | EC:1.1.1.86 | - | 9.699e-22 | - |
Source | KEGGs | Term | Type | e value | Identity |
---|---|---|---|---|---|
Sma3 | Valine, leucine and isoleucine biosynthesis | 00290 | 9.699e-22 | % | |
Sma3 | Pantothenate and CoA biosynthesis | 00770 | 9.699e-22 | % | |
Sma3 | Biosynthesis of alkaloids derived from histidine and purine | 01065 | 9.699e-22 | % | |
Sma3 | Metabolic pathways | 01100 | 9.699e-22 | % | |
Sma3 | Biosynthesis of secondary metabolites | 01110 | 9.699e-22 | % |
Source | Gene names |
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Sma3 | 1B08; AAI1; AHRI; AT3G58610; At3g58610; CHLREDRAFT_140839; F14P22.200; GSVIVT00018719001; GSVIVT00035885001; LOC_Os10g30970; MICPUCDRAFT_49717; MICPUN_57653; OJ1735_C10.18; OSJNBa0050G13.26; OSJNBb0032K15.18; OSTLU_30575; Os01g0652600; Os02g0151600; Os05g |
Source | GOs | Term | Type | e value | Identity |
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Sma3 | cell wall | GO:0005618 | Cellular Component | 0.0 | - |
Sma3 | mitochondrion | GO:0005739 | Cellular Component | 0.0 | - |
Sma3 | chloroplast | GO:0009507 | Cellular Component | 0.0 | - |
Sma3 | chloroplast stroma | GO:0009570 | Cellular Component | 0.0 | - |
Sma3 | chloroplast envelope | GO:0009941 | Cellular Component | 0.0 | - |
Sma3 | apoplast | GO:0048046 | Cellular Component | 0.0 | - |
Sma3 | magnesium ion binding | GO:0000287 | Molecular Function | 0.0 | - |
Sma3 | ketol-acid reductoisomerase activity | GO:0004455 | Molecular Function | 0.0 | - |
Sma3 | binding | GO:0005488 | Molecular Function | 0.0 | - |
Sma3 | isomerase activity | GO:0016853 | Molecular Function | 0.0 | - |
Sma3 | coenzyme binding | GO:0050662 | Molecular Function | 0.0 | - |
Sma3 | cellular amino acid biosynthetic process | GO:0008652 | Biological Process | 0.0 | - |
Sma3 | branched chain family amino acid biosynthetic process | GO:0009082 | Biological Process | 0.0 | - |
Sma3 | response to cadmium ion | GO:0046686 | Biological Process | 0.0 | - |
Sma3 | oxidation-reduction process | GO:0055114 | Biological Process | 0.0 | - |
Source | InterPros | Term | Type | e value | Identity |
---|---|---|---|---|---|
Sma3 | Acetohydroxy acid isomeroreductase C-terminal | IPR000506 | - | 0.0 | - |
Sma3 | Phosphopantetheine attachment site | IPR006162 | - | 0.0 | - |
Sma3 | Acetohydroxy acid isomeroreductase | IPR013023 | - | 0.0 | - |
Sma3 | Acetohydroxy acid isomeroreductase, catalytic | IPR013116 | - | 0.0 | - |
Sma3 | Dehydrogenase, multihelical | IPR013328 | - | 0.0 | - |
Sma3 | NAD(P)-binding domain | IPR016040 | - | 0.0 | - |
Sma3 | Ketol-acid reductoisomerase | IPR016206 | - | 0.0 | - |
Source | Species | ID | Description | e value | Identity |
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ATG | Arabidoptis thaliana | AT3G58610.1 | ketol-acid reductoisomerase chr3:21671561-21674639 FORWARD LENGTH=591 | 1.0e-28 | 83% |
RefSeq | Arabidopsis thaliana | NP_001190127.1 | ketol-acid reductoisomerase [Arabidopsis thaliana] | 2.0e-28 | 83% |
RefSeq | Populus trichocarpa | XP_002305797.1 | predicted protein [Populus trichocarpa] | 1.0e-28 | 85% |
Full-Lengther Next Prediction |
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Fln status: Internal
Fln database: coniferopsida.fasta
Fln subject: B8LR30
Fln msg: Distance to subject end: 262 aas, your sequence is shorter than subject: 80 - 467
Fln protein:
G
Protein Length:
81
Fln nts:
G
Fln Alignment:
biogeco1_euler_14121___GVIGWGSQGPAQAQNLRDSLAEAKSGIVVKVGLRKGSKSFAEACAAGFSXXXXXXXXXXXXXXGSDLVLLLISDAAQADN
B8LR30________________GVIGWGSQGPAQAQNLRDSLVEAKSDIVVKIGLRKGSKSFAEARAAGFSEENGTLGEMIETVSGSDLVLLLISDAAQADN
Biología Molecular y Biotecnología de Plantas, Facultad de Ciencias y Plataforma Andaluza de Bioinformática, Universidad de Málaga, E-29071 Málaga, Spain