Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9T0N8 (CKX1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytokinin dehydrogenase 1
EC=1.5.99.12
Alternative name(s):
Cytokinin oxidase 1
Short name=CKO 1
Short name=COX 1
ZmCKX1
Gene names
Name:CKX1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group. Cleaves zeatin, isopentenyladenine, isopentenyladenosine, zeatin riboside and cis-zeatin, but not dihydrozeatin, kinetin and benzylaminopurine.

Catalytic activity

N(6)-dimethylallyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor.

Cofactor

FAD.

Enzyme regulation

Competitive inhibition by phenylureas.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted › extracellular space.

Tissue specificity

Expressed in immature kernels and unpollinated cobs. Weakly expressed in kernels harvested two weeks after anthesis. Ref.3

Post-translational modification

Glycosylated; with approximately 10 hexose residues per site.

Sequence similarities

Belongs to the oxygen-dependent FAD-linked oxidoreductase family.

Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcytokinin metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionUDP-N-acetylmuramate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

cytokinin dehydrogenase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 534516Cytokinin dehydrogenase 1
PRO_0000020424

Regions

Domain65 – 245181FAD-binding PCMH-type
Nucleotide binding100 – 1045FAD By similarity
Nucleotide binding105 – 1062FAD By similarity
Nucleotide binding180 – 1845FAD By similarity
Nucleotide binding527 – 5304FAD By similarity
Compositional bias339 – 3457Poly-Ala

Sites

Binding site1101FAD; via carbonyl oxygen By similarity
Binding site1691FAD; via amide nitrogen By similarity
Binding site1741FAD By similarity
Binding site2351FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4911FAD By similarity

Amino acid modifications

Modified residue1051Pros-8alpha-FAD histidine
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation4341N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict791G → A in CAA77151. Ref.1
Sequence conflict1681N → T in CAA77151. Ref.1
Sequence conflict2541F → L in CAA77151. Ref.1

Secondary structure

1 ................................................................................... 534
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9T0N8 [UniParc].

Last modified May 24, 2005. Version 2.
Checksum: 13FB5AF654C169E5

FASTA53457,229
        10         20         30         40         50         60 
MAVVYYLLLA GLIACSHALA AGTPALGDDR GRPWPASLAA LALDGKLRTD SNATAAASTD 

        70         80         90        100        110        120 
FGNITSALPA AVLYPSSTGD LVALLSAANS TPGWPYTIAF RGRGHSLMGQ AFAPGGVVVN 

       130        140        150        160        170        180 
MASLGDAAAP PRINVSADGR YVDAGGEQVW IDVLRASLAR GVAPRSWNDY LYLTVGGTLS 

       190        200        210        220        230        240 
NAGISGQAFR HGPQISNVLE MDVITGHGEM VTCSKQLNAD LFDAVLGGLG QFGVITRARI 

       250        260        270        280        290        300 
AVEPAPARAR WVRFVYTDFA AFSADQERLT APRPGGGGAS FGPMSYVEGS VFVNQSLATD 

       310        320        330        340        350        360 
LANTGFFTDA DVARIVALAG ERNATTVYSI EATLNYDNAT AAAAAVDQEL ASVLGTLSYV 

       370        380        390        400        410        420 
EGFAFQRDVA YAAFLDRVHG EEVALNKLGL WRVPHPWLNM FVPRSRIADF DRGVFKGILQ 

       430        440        450        460        470        480 
GTDIVGPLIV YPLNKSMWDD GMSAATPSED VFYAVSLLFS SVAPNDLARL QEQNRRILRF 

       490        500        510        520        530 
CDLAGIQYKT YLARHTDRSD WVRHFGAAKW NRFVEMKNKY DPKRLLSPGQ DIFN

« Hide

References

[1]"Cytokinin oxidase from Zea mays: purification, cDNA cloning and expression in moss protoplasts."
Houba-Herin N., Pethe C., D'Alayer J., Laloue M.
Plant J. 17:615-626(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 417-435; 490-517 AND 524-534.
Strain: cv. Nobilis.
Tissue: Kernel.
[2]"Isolation of a gene encoding a glycosylated cytokinin oxidase from maize."
Morris R.O., Bilyeu K.D., Laskey J.G., Cheikh N.N.
Biochem. Biophys. Res. Commun. 255:328-333(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 286-308; 369-377; 388-392 AND 417-431, MASS SPECTROMETRY.
[3]"Molecular and biochemical characterization of a cytokinin oxidase from maize."
Bilyeu K.D., Cole J.L., Laskey J.G., Riekhof W.R., Esparza T.J., Kramer M.D., Morris R.O.
Plant Physiol. 125:378-386(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
[4]"Structure and function of cytokinin oxidase/dehydrogenase genes of maize, rice, Arabidopsis and other species."
Schmuelling T., Werner T., Riefler M., Krupkova E., Bartrina y Manns I.
J. Plant Res. 116:241-252(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, NOMENCLATURE.
[5]"Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis."
Malito E., Coda A., Bilyeu K.D., Fraaije M.W., Mattevi A.
J. Mol. Biol. 341:1237-1249(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-534 OF APOENZYME AND IN COMPLEX WITH BENZYLAMINOPURINE; ISOPENTENYLADENINE OR TRANS-ZEATIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y18377 mRNA. Translation: CAA77151.1.
AF044603 Genomic DNA. Translation: AAC27500.1.
PIRT01500.
T51929.
RefSeqNP_001105591.1. NM_001112121.1.
UniGeneZm.209.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1OX-ray1.70A1-534[»]
1W1QX-ray1.80A1-534[»]
1W1RX-ray1.90A1-534[»]
1W1SX-ray2.00A1-534[»]
2QKNX-ray2.15A19-534[»]
2QPMX-ray1.85A19-534[»]
3BW7X-ray1.95A19-534[»]
3C0PX-ray1.95A19-534[»]
3DQ0X-ray1.90A19-534[»]
3KJMX-ray1.90A19-534[»]
3S1CX-ray2.09A19-534[»]
3S1DX-ray1.75A19-534[»]
3S1EX-ray1.90A19-534[»]
3S1FX-ray2.00A19-534[»]
ProteinModelPortalQ9T0N8.
SMRQ9T0N8. Positions 32-534.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542585.
KEGGzma:542585.

Organism-specific databases

GrameneQ9T0N8.
MaizeGDB194080.

Phylogenomic databases

KOK00279.

Enzyme and pathway databases

BioCycMetaCyc:CKX1-MONOMER.
BRENDA1.5.99.12. 6752.
SABIO-RKQ9T0N8.

Family and domain databases

Gene3D3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR015345. Cytokinin_DH_FAD/cytokin-bd.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
IPR016170. V_Alc_oxidase/Cytok_DH_C_dom.
[Graphical view]
PfamPF09265. Cytokin-bind. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. FAD-binding_2. 1 hit.
SSF56176. FAD-binding_2. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL5363.
EvolutionaryTraceQ9T0N8.

Entry information

Entry nameCKX1_MAIZE
AccessionPrimary (citable) accession number: Q9T0N8
Secondary accession number(s): O81158
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: May 24, 2005
Last modified: April 3, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents