Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_32541g0010 |
Family | AA7 |
Protein Properties | Length: 549 Molecular Weight: 61225.3 Isoelectric Point: 5.1397 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 69 | 255 | 1.7e-30 |
HNKPAAVLSPASAEDISKLIRIAATSPNLTIAARGNGHSIGGQAMALNGIVVNMTSLKGINIVDENNTDAPYADVMAGEFWVDVLRATVGAGLAPRSWTD YIDLSIGGTLSIAGISGQTYRFGPQISNVLQLEIVTGNGEIITCSAQNQPDLYFGALGGLGQFGIITKARIILQRAPRRARLIRLVY |
Full Sequence |
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Protein Sequence Length: 549 Download |
MKLRCLVVFL LIALFRRLRG DDTYGDCMIS GDLDQQVCQQ LAAAEFEGPI IFKGPSIEEA 60 SNDFGGIYHN KPAAVLSPAS AEDISKLIRI AATSPNLTIA ARGNGHSIGG QAMALNGIVV 120 NMTSLKGINI VDENNTDAPY ADVMAGEFWV DVLRATVGAG LAPRSWTDYI DLSIGGTLSI 180 AGISGQTYRF GPQISNVLQL EIVTGNGEII TCSAQNQPDL YFGALGGLGQ FGIITKARII 240 LQRAPRRARL IRLVYWKLED FMHDQELLIS LPPGKTFDYI EGFVVVNEDY SINGWSSIPL 300 LSNQSFDGSL IPSTAGPLLY AIEVAHYYDP GMDTDKIIES LLSKLGFIKG LEFSVDLSYF 360 DFLYRVHAEE VAARESGIWY TPHAWFNFFV PKSKMVEFDC KIFKNILING VDGLMLLYPM 420 KRSLWDSRTS AVVPEEDIFY VVSLLRFSKP FPEGPPLSVV LDQNNAILKA CRASGIPVKQ 480 YIGRHETQTE WEKHFGEERW ERFLERKRLF DPKAILAPGQ NIFPRNSIYF LELAPGQNIF 540 PRNSIYFLE |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 2.0e-12 | 66 | 266 | 202 | + 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 | 9.0e-30 | 65 | 522 | 464 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-30 | 72 | 213 | 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 | 2.0e-108 | 245 | 523 | 283 | + 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 | 1 | 527 | 533 | + 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 |
GenBank | ACP40989.1 | 0 | 41 | 526 | 27 | 510 | cytokinin oxidase/dehydrogenase [Solanum tuberosum] |
RefSeq | NP_001146838.1 | 0 | 63 | 525 | 36 | 518 | cytokinin dehydrogenase 10 [Zea mays] |
RefSeq | XP_002279960.1 | 0 | 34 | 526 | 20 | 512 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002309468.1 | 0 | 60 | 527 | 47 | 519 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002516133.1 | 0 | 37 | 527 | 26 | 518 | gulonolactone oxidase, 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 | 47 | 526 | 37 | 523 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 2exr_A | 0 | 47 | 526 | 37 | 523 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 3s1e_A | 0 | 40 | 523 | 19 | 515 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
PDB | 3s1c_A | 0 | 40 | 523 | 19 | 515 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
PDB | 3dq0_A | 0 | 40 | 523 | 19 | 515 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |