y
Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_42031g0010 |
Family | AA7 |
Protein Properties | Length: 542 Molecular Weight: 61203.9 Isoelectric Point: 9.0836 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 74 | 266 | 5.7e-27 |
GNRYSYLPAAVVYPASIRDIKRVVKSVYLSDSCSKLTVSAKGNAHSVQGQAQAPNGIVIEMGSLKGIQVHKEPENPYVEASAGELWIDVLRATLKHGLAP RSWTDYLYLSVGGTLSNAGISGQAFRHGPQISNVYHLQIVTGKGEISNCSREENSDLFYGALGGLGQFGIITSARIALEQAPQMVRWIRVLYS |
Full Sequence |
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Protein Sequence Length: 542 Download |
MKKVAIWVVE NRRLAVLLLF GLARLISAVR FNQDLKFWPS FVSSLQWASL KSLDLDLDGR 60 IAFHNNHNAA KDFGNRYSYL PAAVVYPASI RDIKRVVKSV YLSDSCSKLT VSAKGNAHSV 120 QGQAQAPNGI VIEMGSLKGI QVHKEPENPY VEASAGELWI DVLRATLKHG LAPRSWTDYL 180 YLSVGGTLSN AGISGQAFRH GPQISNVYHL QIVTGKGEIS NCSREENSDL FYGALGGLGQ 240 FGIITSARIA LEQAPQMVRW IRVLYSDFEL FTRDQEYLIS KSDGAYTFDY IEGFVILRNE 300 ALLNNWRSSM FSPQNPGNLS TVSAKGRVLY CLELTKNYNQ NERVNVGQEI NSLLDVLSFI 360 PSSLFTKDIP YVDFLDRVHT EELKLRSRGL WEVPHPWLNL LIPKSKIAEF DAAVFKDMLR 420 NPRDGPILIY PMNRNKWDSR MSAVTPNEDI FYLVAFLRSA IPSSTNHLDN LIDQNQKILS 480 FCQQAGIGAK QYLPHHTTED DWKTHFGEKW DKFVQRKTVY DPTAILAPGQ RIFSKCRAFS 540 VS 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01678 | FAD_lactone_ox | 7.0e-10 | 71 | 249 | 179 | + 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. | ||
COG0277 | GlcD | 3.0e-22 | 74 | 530 | 483 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 1.0e-24 | 81 | 223 | 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. | ||
pfam09265 | Cytokin-bind | 1.0e-151 | 255 | 533 | 281 | + 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 | 43 | 540 | 505 | + 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 | CBI28611.1 | 0 | 55 | 539 | 76 | 558 | unnamed protein product [Vitis vinifera] |
EMBL | CBI33379.1 | 0 | 39 | 542 | 46 | 546 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270841.1 | 0 | 55 | 539 | 46 | 528 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002284560.1 | 0 | 39 | 542 | 26 | 526 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002304773.1 | 0 | 55 | 540 | 33 | 517 | 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 | 3s1c_A | 0 | 48 | 534 | 18 | 516 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 3dq0_A | 0 | 48 | 534 | 18 | 516 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 3c0p_A | 0 | 48 | 534 | 18 | 516 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 3bw7_A | 0 | 48 | 534 | 18 | 516 | A Chain A, Structure Of Mouse Golgi Alpha-1,2-Mannosidase Ia Reveals The Molecular Basis For Substrate Specificity Among Class I Enzymes (Family 47 Glycosidases) |
PDB | 2qkn_A | 0 | 48 | 534 | 18 | 516 | A Chain A, Crystal Structure Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Phenylurea Inhibitor Cppu |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CO160641 | 253 | 26 | 278 | 0 |
HO781924 | 486 | 55 | 535 | 0 |
ES837714 | 294 | 171 | 464 | 0 |
DY269838 | 331 | 81 | 399 | 0 |
GT243083 | 204 | 339 | 542 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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