Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10433485g0010 |
Family | AA7 |
Protein Properties | Length: 857 Molecular Weight: 95031.1 Isoelectric Point: 6.5699 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 392 | 580 | 1.5e-28 |
ARPTAVLYPESITDIVTMVKSTYRCASSSNLTIAAKGHAHSVNGQAQAENGIVIEMGSLKGSIDVNSKGLYVDVNGGELWIDVLHATLKERLAPKSWTDY LYLTVGGTLSVPGISGQVFRHGPHINNVHQLEVVTGKGNLLKCSKDQNTELFHAVLGGLGQFGIITKARIALEPAPQRVRWIRVLYSNF |
Full Sequence |
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Protein Sequence Length: 857 Download |
MENRTSVLVL IFVITSLISA VGLSSLDFGC SPLRTLNFDG HVDFDNTHLA ATDFGNRHRT 60 HPRAVLYPAS VSDIATLVKS TYRCGSLSDL TIAAKGHAHS LNGQAQAENG IVIEMGSLKG 120 VIDVESQGLY VDVNGGELWI DVLHATLKEG LAPKSWTDYL YLTVGGTLLA PKSWTDYLYL 180 TVGGTLSNAG ISGQAFRHGP QINNVYQLEV VTGKGDVLNC SKDQNTELFH AVLGGLGQFG 240 IITKARIALE PAPQRVRWIR VLYADFKAFT TDQEYLISRP RGDLTFDYVE GFVVVNNEGL 300 LSNWRSSFFS PQNPVDYSAI GDFGADIDLR DHMENQISVL ILIFVITSLI SAVGLMVLEL 360 GCSPLRTLDL DGHVDFDNTH VAASDFGNLR RARPTAVLYP ESITDIVTMV KSTYRCASSS 420 NLTIAAKGHA HSVNGQAQAE NGIVIEMGSL KGSIDVNSKG LYVDVNGGEL WIDVLHATLK 480 ERLAPKSWTD YLYLTVGGTL SVPGISGQVF RHGPHINNVH QLEVVTGKGN LLKCSKDQNT 540 ELFHAVLGGL GQFGIITKAR IALEPAPQRV RWIRVLYSNF KTFTKDQEHL ISRQNGDLTV 600 DYVEGFVIVN NEGLLSNWRS SFFSPQNPEK AKYLNTKGRV LYCLEMAMNH MNNDTIMVDE 660 DVTFLLSSLH FIPGSVFITD VSYVEFLDRV HTSELKLRSQ DLWEVPHPWL NLFVPGSKIH 720 EFDARVFKDI LRNTSSGPIL IYPMNSNTWD KRMSAVTPEE NIFYLVGLLR SSLPSATGSN 780 SVEYLMDQNI RILNFCNKAG IGAKQYLPHY TTESEWEKHF GTKWYRFVDL KEKYDPHAIL 840 APGQRIFSRT ARASPLS |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01565 | FAD_binding_4 | 9.0e-25 | 394 | 535 | 143 | + 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 | 3.0e-26 | 253 | 321 | 69 | + 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. | ||
pfam09265 | Cytokin-bind | 1.0e-151 | 567 | 847 | 282 | + 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 | 2.0e-167 | 8 | 320 | 321 | + cytokinin dehydrogenase | ||
PLN02441 | PLN02441 | 0 | 340 | 854 | 523 | + 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 | CBI19763.1 | 0 | 8 | 325 | 60 | 362 | unnamed protein product [Vitis vinifera] |
EMBL | CBI19763.1 | 0 | 330 | 854 | 53 | 578 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002280797.1 | 0 | 8 | 325 | 5 | 307 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002280797.1 | 0 | 340 | 854 | 5 | 523 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002284560.1 | 0 | 363 | 854 | 35 | 524 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 365 | 848 | 20 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3s1d_A | 0 | 33 | 310 | 20 | 290 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3s1c_A | 0 | 365 | 848 | 20 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3s1c_A | 0 | 33 | 310 | 20 | 290 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3dq0_A | 0 | 365 | 848 | 20 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |