Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_5215129g0010 |
Family | AA7 |
Protein Properties | Length: 238 Molecular Weight: 25289.8 Isoelectric Point: 5.2178 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 53 | 237 | 4.9e-28 |
DFGNRLTAHPTAVLYPASVSDIATLVKSIYSCGSSSDLTVAAKGHAHSLNGQAQAENGIVIEMESLKGLIDVKSQDLSYVDVNGGELWIDVLHATLKEGL APKSWTDYLYLTVGGTLSNAGISGQAFRHGPQINNVYQLEVVTGKGDVLKCSKDQNTELFLAVLGGLGQFGIITKARIALEPAPQ |
Full Sequence |
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Protein Sequence Length: 238 Download |
MENRTSVLVL IFVITSLISA VGLVTLDLGC LPLRALDFDG HVDFDNTHLA ATDFGNRLTA 60 HPTAVLYPAS VSDIATLVKS IYSCGSSSDL TVAAKGHAHS LNGQAQAENG IVIEMESLKG 120 LIDVKSQDLS YVDVNGGELW IDVLHATLKE GLAPKSWTDY LYLTVGGTLS NAGISGQAFR 180 HGPQINNVYQ LEVVTGKGDV LKCSKDQNTE LFLAVLGGLG QFGIITKARI ALEPAPQR 240 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01678 | FAD_lactone_ox | 3.0e-8 | 59 | 235 | 178 | + sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. | ||
TIGR01679 | bact_FAD_ox | 6.0e-10 | 59 | 230 | 172 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. | ||
COG0277 | GlcD | 2.0e-21 | 39 | 238 | 207 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 7.0e-24 | 62 | 204 | 144 | + FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. | ||
PLN02441 | PLN02441 | 7.0e-139 | 8 | 238 | 238 | + cytokinin dehydrogenase |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002270841.1 | 0 | 12 | 237 | 16 | 248 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002284560.1 | 0 | 33 | 237 | 37 | 242 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002304773.1 | 0 | 7 | 236 | 2 | 234 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002323274.1 | 0 | 33 | 237 | 57 | 262 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002332424.1 | 0 | 10 | 236 | 14 | 247 | cytokinin oxidase [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3s1d_A | 0 | 33 | 238 | 20 | 230 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3kjm_A | 0 | 33 | 238 | 20 | 230 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 2qpm_A | 0 | 33 | 238 | 20 | 230 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
PDB | 3s1c_A | 0 | 33 | 238 | 20 | 230 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
PDB | 3dq0_A | 0 | 33 | 238 | 20 | 230 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |