Q9T0N8 · CKX1_MAIZE
- ProteinCytokinin dehydrogenase 1
- GeneCKX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids534 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidation of cytokinins, a family of N6-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group (PubMed:11154345).
Cleaves trans-zeatin, N6-dimethylallyladenine (isopentenyladenine), isopentenyladenosine, zeatin riboside and cis-zeatin, but not dihydrozeatin, kinetin and benzylaminopurine (PubMed:11154345).
Cleaves trans-zeatin, N6-dimethylallyladenine (isopentenyladenine), isopentenyladenosine, zeatin riboside and cis-zeatin, but not dihydrozeatin, kinetin and benzylaminopurine (PubMed:11154345).
Catalytic activity
- A + H2O + N6-dimethylallyladenine = 3-methyl-2-butenal + adenine + AH2
Cofactor
Activity regulation
Competitive inhibition by phenylureas.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 100 | FAD (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 102 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 103 | FAD (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 104 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 106 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 110 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 169 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 169 | N6-dimethylallyladenine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 169 | trans-zeatin (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 174 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 180 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 184 | FAD (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 235 | FAD (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 381 | N6-dimethylallyladenine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 381 | trans-zeatin (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 456 | trans-zeatin (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 491 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 527 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 530 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | cytokinin dehydrogenase activity | |
Molecular Function | FAD binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | cytokinin metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytokinin dehydrogenase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea
Accessions
- Primary accessionQ9T0N8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MAVVYYLLLAGLIACSHA | ||||||
Chain | PRO_0000020424 | 19-534 | Cytokinin dehydrogenase 1 | |||
Sequence: LAAGTPALGDDRGRPWPASLAALALDGKLRTDSNATAAASTDFGNITSALPAAVLYPSSTGDLVALLSAANSTPGWPYTIAFRGRGHSLMGQAFAPGGVVVNMASLGDAAAPPRINVSADGRYVDAGGEQVWIDVLRASLARGVAPRSWNDYLYLTVGGTLSNAGISGQAFRHGPQISNVLEMDVITGHGEMVTCSKQLNADLFDAVLGGLGQFGVITRARIAVEPAPARARWVRFVYTDFAAFSADQERLTAPRPGGGGASFGPMSYVEGSVFVNQSLATDLANTGFFTDADVARIVALAGERNATTVYSIEATLNYDNATAAAAAVDQELASVLGTLSYVEGFAFQRDVAYAAFLDRVHGEEVALNKLGLWRVPHPWLNMFVPRSRIADFDRGVFKGILQGTDIVGPLIVYPLNKSMWDDGMSAATPSEDVFYAVSLLFSSVAPNDLARLQEQNRRILRFCDLAGIQYKTYLARHTDRSDWVRHFGAAKWNRFVEMKNKYDPKRLLSPGQDIFN | ||||||
Glycosylation | 52 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 63 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 89 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 105 | Pros-8alpha-FAD histidine | ||||
Sequence: H | ||||||
Glycosylation | 134 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 294 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 323 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 338 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 434 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated; with approximately 10 hexose residues per site.
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed in immature kernels and unpollinated cobs. Weakly expressed in kernels harvested two weeks after anthesis.
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 65-245 | FAD-binding PCMH-type | ||||
Sequence: TSALPAAVLYPSSTGDLVALLSAANSTPGWPYTIAFRGRGHSLMGQAFAPGGVVVNMASLGDAAAPPRINVSADGRYVDAGGEQVWIDVLRASLARGVAPRSWNDYLYLTVGGTLSNAGISGQAFRHGPQISNVLEMDVITGHGEMVTCSKQLNADLFDAVLGGLGQFGVITRARIAVEPA |
Sequence similarities
Belongs to the oxygen-dependent FAD-linked oxidoreductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length534
- Mass (Da)57,229
- Last updated2005-05-24 v2
- Checksum13FB5AF654C169E5
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 79 | in Ref. 1; CAA77151 | ||||
Sequence: G → A | ||||||
Sequence conflict | 168 | in Ref. 1; CAA77151 | ||||
Sequence: N → T | ||||||
Sequence conflict | 254 | in Ref. 1; CAA77151 | ||||
Sequence: F → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y18377 EMBL· GenBank· DDBJ | CAA77151.1 EMBL· GenBank· DDBJ | mRNA | ||
AF044603 EMBL· GenBank· DDBJ | AAC27500.1 EMBL· GenBank· DDBJ | Genomic DNA |