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Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr1g015410.1 |
Family | AA7 |
Protein Properties | Length: 510 Molecular Weight: 56766.7 Isoelectric Point: 6.9034 |
Chromosome | Chromosome/Scaffold: 1 Start: 4243565 End: 4248963 |
Description | cytokinin oxidase 7 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 45 | 236 | 3.2e-28 |
KSSTPLAVLRPYTTADVVKAVKAAATTTNLTVAARGNGHSINGQAMAEKGLVLDMRATAAEPFQLLYVDGVPHVDVSGGALWEEVLKRCVSNFQLVPRSW TDYLGLTVGGTLSNAGVSGQTFRYGPQTANVTELEVVTGKGDSFVCNDNQNSDLFFASLGGLGQFGVITRARIVLQQAPDMVRWIRVIYSEF |
Full Sequence |
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Protein Sequence Length: 510 Download |
MIAYLEHFVH GNDTESPPND DVSSLQSSFH FAPNSIASKD FGGMKSSTPL AVLRPYTTAD 60 VVKAVKAAAT TTNLTVAARG NGHSINGQAM AEKGLVLDMR ATAAEPFQLL YVDGVPHVDV 120 SGGALWEEVL KRCVSNFQLV PRSWTDYLGL TVGGTLSNAG VSGQTFRYGP QTANVTELEV 180 VTGKGDSFVC NDNQNSDLFF ASLGGLGQFG VITRARIVLQ QAPDMVRWIR VIYSEFEDYT 240 RDAEWLVTLP EGDGFDYVEG FVVANNDDPC NGWPTIPMGS NQIFNPVCLP SSAGPVLYCL 300 ELALHYRKTA RSSEVNTKVD RLLGGLRFVE GIKFEDDVKY MDFLLRVKRV EEDAKAKGIW 360 DAPHPWLNMF VSKSDIADFD REVFKKILKH GVGGPILVYP LLRSKWDDRH SVVVPDSNIF 420 YIIALLRFIP PPPKGPPTDK LVAQNNAIIQ LCYNKGFNFK LYLPHYTSQE NWMRHFGDRW 480 TRFVQRKQNF DPMAILAPGQ KIFSRNQLK* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01565 | FAD_binding_4 | 5.0e-14 | 79 | 191 | 115 | + 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 | 8.0e-18 | 79 | 500 | 429 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam09265 | Cytokin-bind | 7.0e-126 | 223 | 503 | 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 | 0 | 1 | 506 | 515 | + cytokinin dehydrogenase |
Gene Ontology | |
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GO Term | Description |
GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
GO:0009690 | cytokinin metabolic process |
GO:0016491 | oxidoreductase activity |
GO:0019139 | cytokinin dehydrogenase activity |
GO:0050660 | flavin adenine dinucleotide binding |
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 | ABK32520.1 | 0 | 1 | 500 | 1 | 500 | cytokinin oxidase/dehydrogenase 1 [Pisum sativum] |
RefSeq | NP_850863.1 | 0 | 1 | 506 | 1 | 523 | CKX7 (CYTOKININ OXIDASE 7); cytokinin dehydrogenase/ oxidoreductase [Arabidopsis thaliana] |
RefSeq | XP_002279960.1 | 0 | 1 | 507 | 1 | 513 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002309468.1 | 0 | 1 | 505 | 1 | 517 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002516133.1 | 0 | 1 | 506 | 1 | 517 | 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 | 32 | 506 | 45 | 523 | A Chain A, Crystal Structure Of Rice Bglu1 E386gS334A MUTANT COMPLEXED WITH Cellotetraose |
PDB | 2exr_A | 0 | 32 | 506 | 45 | 523 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 3s1d_A | 0 | 34 | 504 | 36 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3s1c_A | 0 | 34 | 504 | 36 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3dq0_A | 0 | 34 | 504 | 36 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO781924 | 503 | 1 | 503 | 0 |
FY455456 | 247 | 114 | 360 | 0 |
BG582321 | 237 | 89 | 324 | 0 |
BG456140 | 218 | 93 | 310 | 0 |
BG582321 | 25 | 317 | 341 | 0.00003 |
Sequence Alignments (This image is cropped. Click for full image.) |
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