Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi2g05580.1 |
Family | AA7 |
Protein Properties | Length: 522 Molecular Weight: 55393.7 Isoelectric Point: 5.3174 |
Chromosome | Chromosome/Scaffold: 2 Start: 4063596 End: 4066579 |
Description | cytokinin oxidase 5 |
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 | 65 | 518 | 2.4e-25 |
SALPAAVLFPSSPADIAALLRAAAGKVSFRGRGHSVMGQALAPGGVVVDMPSLGLGLGLSGARINVSADGGYVDAGGEQQWIDVLRAALRQGVAPRSWTD YLRLTVGGTLSNAGISGQAFRHGPQISNVLELDVITGNGETVTCSKSENADLFDAALGGLGQFGVIVRARIPLEPAPARARWVRLVYTDFATFSADQERV IAGAADSAFGAVSYLEGAAYVNQSLASGLKNAGGFYSDADVSRIVALAALRNASSLYAIELTLNYVNATAVDQEFEAVVGELRHETGFAFARDVAYEAFL DRVYEEEVALEKLGLWRVPHPWLNVLVPSSRIADFDRAVFKGILQGTDIAGPLVIYPLNKSKWDEGMSAVTPAEEVFYAVSLLFSSVANDLKKLQAQNQK ILQFCDMAGIGYKEYLAHYTTRGDWARHFGDKWDRFVQRKDKYDPKKLLCPGQD |
Full Sequence |
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Protein Sequence Length: 522 Download |
MAAAYVLALA ALLALASSSS QQYANAQASL LHGDDALAAL AAAGKLRTDA TATAAASTDF 60 GNITSALPAA VLFPSSPADI AALLRAAAGK VSFRGRGHSV MGQALAPGGV VVDMPSLGLG 120 LGLSGARINV SADGGYVDAG GEQQWIDVLR AALRQGVAPR SWTDYLRLTV GGTLSNAGIS 180 GQAFRHGPQI SNVLELDVIT GNGETVTCSK SENADLFDAA LGGLGQFGVI VRARIPLEPA 240 PARARWVRLV YTDFATFSAD QERVIAGAAD SAFGAVSYLE GAAYVNQSLA SGLKNAGGFY 300 SDADVSRIVA LAALRNASSL YAIELTLNYV NATAVDQEFE AVVGELRHET GFAFARDVAY 360 EAFLDRVYEE EVALEKLGLW RVPHPWLNVL VPSSRIADFD RAVFKGILQG TDIAGPLVIY 420 PLNKSKWDEG MSAVTPAEEV FYAVSLLFSS VANDLKKLQA QNQKILQFCD MAGIGYKEYL 480 AHYTTRGDWA RHFGDKWDRF VQRKDKYDPK KLLCPGQDIF N* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01678 | FAD_lactone_ox | 5.0e-8 | 169 | 240 | 72 | + 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. | ||
pfam01565 | FAD_binding_4 | 3.0e-18 | 68 | 209 | 146 | + 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 | 5.0e-24 | 66 | 517 | 465 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam09265 | Cytokin-bind | 4.0e-131 | 241 | 520 | 286 | + 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 | 60 | 521 | 472 | + 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 |
PDB | 1W1O | 0 | 1 | 521 | 1 | 534 | A Chain A, Native Cytokinin Dehydrogenase |
GenBank | ADB45878.1 | 0 | 1 | 521 | 1 | 525 | cytokinin oxidase/dehydrogenase [Bambusa oldhamii] |
GenBank | ADB45880.1 | 0 | 1 | 521 | 1 | 522 | cytokinin oxidase/dehydrogenase [Bambusa oldhamii] |
RefSeq | NP_001105591.1 | 0 | 1 | 521 | 1 | 534 | cytokinin oxidase1 precursor [Zea mays] |
Swiss-Prot | Q9T0N8 | 0 | 1 | 521 | 1 | 534 | CKX1_MAIZE RecName: Full=Cytokinin dehydrogenase 1; AltName: Full=Cytokinin oxidase 1; Short=CKO 1; Short=COX 1; AltName: Full=ZmCKX1; Flags: Precursor |
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 | 1w1s_A | 0 | 1 | 521 | 1 | 534 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 1w1r_A | 0 | 1 | 521 | 1 | 534 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 1w1q_A | 0 | 1 | 521 | 1 | 534 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 1w1o_A | 0 | 1 | 521 | 1 | 534 | A Chain A, Native Cytokinin Dehydrogenase |
PDB | 3s1c_A | 0 | 36 | 521 | 19 | 516 | A Chain A, Native Cytokinin Dehydrogenase |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cytokinins degradation | RXN-4621 | EC-1.5.99 | isopentenyladenine:FAD oxidoreductase |
cytokinins degradation | RXN-4641 | EC-1.5.99 | isopentenyl adenosine:FAD oxidoreductase |
cytokinins degradation | RXN-4661 | EC-1.5.99 | trans-zeatin:FAD oxidoreductase |
cytokinins degradation | RXN-4662 | EC-1.5.99 | cis-zeatin:FAD oxidoreductase |
cytokinins degradation | RXN-4681 | EC-1.5.99 | trans-zeatin riboside:FAD oxidoreductase |