Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_17212g0010 |
Family | AA7 |
Protein Properties | Length: 552 Molecular Weight: 61095.5 Isoelectric Point: 6.2464 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 69 | 269 | 9.4e-30 |
HHNPAAILRPASAEEIARFLRAIYTSRAPAYGQEYLTVAAKGAGHSIHGQAQAPDGLVIEMTSLRGVRIHETDDAGDCSYADVAAGELWIDLLTETMKVG LAPRSWTDYLYLSVGGTLSNAGISGQTFRHGPQISNVLQLDIITGTGELVTCSASENADLFYASMGGLGQFGVITRARIILEPAPHKVKWVRALYSDFEQ F |
Full Sequence |
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Protein Sequence Length: 552 Download |
MGSCNGGLSA LILISMTPPP RVGVLILTAK IRVVYPSYSE KCNTDGQDPR RLSFLDTASA 60 AIDFGKIYHH NPAAILRPAS AEEIARFLRA IYTSRAPAYG QEYLTVAAKG AGHSIHGQAQ 120 APDGLVIEMT SLRGVRIHET DDAGDCSYAD VAAGELWIDL LTETMKVGLA PRSWTDYLYL 180 SVGGTLSNAG ISGQTFRHGP QISNVLQLDI ITGTGELVTC SASENADLFY ASMGGLGQFG 240 VITRARIILE PAPHKVKWVR ALYSDFEQFT RDQELLVSMD EGAATVDYLE GFVVVNNEAM 300 RSWSISFPST TPLNDSVFND AGTEIFFCIE IAKYFTQVDD ETADVDKVMG RIISRLSFIP 360 RLIYSVEVPY ADFLNRVRVE ESNLRSRGLW DVPHPWLNMF VPRRQIQRFT ASLLKIMSPD 420 TVKGPILVYP VNRSKWNTNM SAVIPEDKDE IFYAVGVLRS ADPLCLSGSS CLNDLLSQNQ 480 QIIDLSTKAD GITGDKTDSG MGAKQYLAHH SHEWQWKNHF GSKWGIFLER KARYDPLNIL 540 APGQRILNRN RA |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 3.0e-11 | 69 | 269 | 207 | + 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. | ||
pfam01565 | FAD_binding_4 | 1.0e-25 | 72 | 221 | 151 | + 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. | ||
COG0277 | GlcD | 7.0e-28 | 46 | 544 | 510 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam09265 | Cytokin-bind | 3.0e-121 | 253 | 546 | 298 | + Cytokinin dehydrogenase 1, FAD and cytokinin binding. Members of this family adopt an alpha+beta sandwich structure with an antiparallel beta-sheet, in a ferredoxin-like fold. They are predominantly found in plant cytokinin dehydrogenase 1, where they are capable of binding both FAD and cytokinin substrates. The substrate displays a 'plug-into-socket' binding mode that seals the catalytic site and precisely positions the carbon atom undergoing oxidation in close contact with the reactive locus of the flavin. | ||
PLN02441 | PLN02441 | 0 | 51 | 550 | 506 | + 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 |
EMBL | CAE05712.2 | 0 | 57 | 550 | 40 | 526 | OSJNBb0065J09.8 [Oryza sativa (japonica cultivar-group)] |
EMBL | CBI33379.1 | 0 | 51 | 549 | 65 | 539 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284560.1 | 0 | 51 | 549 | 45 | 519 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002467062.1 | 0 | 57 | 550 | 41 | 515 | hypothetical protein SORBIDRAFT_01g019000 [Sorghum bicolor] |
RefSeq | XP_002513118.1 | 0 | 27 | 549 | 28 | 525 | Cytokinin dehydrogenase, putative [Ricinus communis] |
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 | 2q4w_A | 0 | 60 | 550 | 50 | 523 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 2exr_A | 0 | 60 | 550 | 50 | 523 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 3s1c_A | 0 | 57 | 548 | 36 | 516 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 3dq0_A | 0 | 57 | 548 | 36 | 516 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 3c0p_A | 0 | 57 | 548 | 36 | 516 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO781924 | 499 | 52 | 547 | 0 |
ES837714 | 296 | 169 | 463 | 0 |
DY269838 | 340 | 72 | 398 | 0 |
DT748999 | 247 | 67 | 310 | 0 |
DY963441 | 311 | 51 | 360 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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