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Protein

Cytokinin dehydrogenase 1

Gene

CKX1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Enzyme regulationi

Competitive inhibition by phenylureas.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei110FAD; via carbonyl oxygenBy similarity1
Binding sitei169FAD; via amide nitrogenBy similarity1
Binding sitei174FADBy similarity1
Binding sitei235FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei491FADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi100 – 104FADBy similarity5
Nucleotide bindingi105 – 106FADBy similarity2
Nucleotide bindingi180 – 184FADBy similarity5
Nucleotide bindingi527 – 530FADBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:CKX1-MONOMER.
BRENDAi1.5.99.12. 6752.
SABIO-RKQ9T0N8.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CKX1
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi194080.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5363.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000002042419 – 534Cytokinin dehydrogenase 1Add BLAST516

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Glycosylationi63N-linked (GlcNAc...)Sequence analysis1
Modified residuei105Pros-8alpha-FAD histidine1
Glycosylationi134N-linked (GlcNAc...)Sequence analysis1
Glycosylationi294N-linked (GlcNAc...)Sequence analysis1
Glycosylationi323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi338N-linked (GlcNAc...)Sequence analysis1
Glycosylationi434N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Glycosylated; with approximately 10 hexose residues per site.

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Expressed in immature kernels and unpollinated cobs. Weakly expressed in kernels harvested two weeks after anthesis.1 Publication

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1534
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni41 – 45Combined sources5
Helixi51 – 56Combined sources6
Beta strandi70 – 73Combined sources4
Helixi78 – 90Combined sources13
Beta strandi98 – 103Combined sources6
Beta strandi107 – 109Combined sources3
Beta strandi116 – 120Combined sources5
Helixi121 – 125Combined sources5
Beta strandi127 – 130Combined sources4
Beta strandi132 – 135Combined sources4
Beta strandi139 – 145Combined sources7
Helixi150 – 158Combined sources9
Turni159 – 161Combined sources3
Beta strandi162 – 165Combined sources4
Beta strandi169 – 171Combined sources3
Helixi175 – 179Combined sources5
Helixi188 – 191Combined sources4
Helixi194 – 196Combined sources3
Beta strandi197 – 205Combined sources9
Beta strandi210 – 218Combined sources9
Helixi219 – 225Combined sources7
Beta strandi232 – 244Combined sources13
Beta strandi247 – 257Combined sources11
Helixi259 – 270Combined sources12
Beta strandi285 – 293Combined sources9
Helixi294 – 296Combined sources3
Helixi297 – 302Combined sources6
Beta strandi305 – 307Combined sources3
Helixi309 – 321Combined sources13
Beta strandi325 – 336Combined sources12
Helixi345 – 354Combined sources10
Beta strandi364 – 370Combined sources7
Helixi371 – 375Combined sources5
Helixi377 – 387Combined sources11
Beta strandi391 – 393Combined sources3
Beta strandi398 – 403Combined sources6
Helixi404 – 406Combined sources3
Helixi407 – 414Combined sources8
Turni415 – 421Combined sources7
Beta strandi428 – 434Combined sources7
Helixi435 – 437Combined sources3
Beta strandi448 – 457Combined sources10
Helixi466 – 483Combined sources18
Beta strandi489 – 492Combined sources4
Helixi498 – 505Combined sources8
Helixi507 – 520Combined sources14
Helixi528 – 530Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9T0N8.
SMRiQ9T0N8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9T0N8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini65 – 245FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST181

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi339 – 345Poly-Ala7

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

KOiK00279.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProiIPR016169. 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]
PfamiPF09265. Cytokin-bind. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9T0N8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVVYYLLLA GLIACSHALA AGTPALGDDR GRPWPASLAA LALDGKLRTD
60 70 80 90 100
SNATAAASTD FGNITSALPA AVLYPSSTGD LVALLSAANS TPGWPYTIAF
110 120 130 140 150
RGRGHSLMGQ AFAPGGVVVN MASLGDAAAP PRINVSADGR YVDAGGEQVW
160 170 180 190 200
IDVLRASLAR GVAPRSWNDY LYLTVGGTLS NAGISGQAFR HGPQISNVLE
210 220 230 240 250
MDVITGHGEM VTCSKQLNAD LFDAVLGGLG QFGVITRARI AVEPAPARAR
260 270 280 290 300
WVRFVYTDFA AFSADQERLT APRPGGGGAS FGPMSYVEGS VFVNQSLATD
310 320 330 340 350
LANTGFFTDA DVARIVALAG ERNATTVYSI EATLNYDNAT AAAAAVDQEL
360 370 380 390 400
ASVLGTLSYV EGFAFQRDVA YAAFLDRVHG EEVALNKLGL WRVPHPWLNM
410 420 430 440 450
FVPRSRIADF DRGVFKGILQ GTDIVGPLIV YPLNKSMWDD GMSAATPSED
460 470 480 490 500
VFYAVSLLFS SVAPNDLARL QEQNRRILRF CDLAGIQYKT YLARHTDRSD
510 520 530
WVRHFGAAKW NRFVEMKNKY DPKRLLSPGQ DIFN
Length:534
Mass (Da):57,229
Last modified:May 24, 2005 - v2
Checksum:i13FB5AF654C169E5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti79G → A in CAA77151 (PubMed:10230061).Curated1
Sequence conflicti168N → T in CAA77151 (PubMed:10230061).Curated1
Sequence conflicti254F → L in CAA77151 (PubMed:10230061).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18377 mRNA. Translation: CAA77151.1.
AF044603 Genomic DNA. Translation: AAC27500.1.
PIRiT01500.
T51929.
RefSeqiNP_001105591.1. NM_001112121.1.
UniGeneiZm.209.

Genome annotation databases

GeneIDi542585.
KEGGizma:542585.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18377 mRNA. Translation: CAA77151.1.
AF044603 Genomic DNA. Translation: AAC27500.1.
PIRiT01500.
T51929.
RefSeqiNP_001105591.1. NM_001112121.1.
UniGeneiZm.209.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9T0N8.
SMRiQ9T0N8.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL5363.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi542585.
KEGGizma:542585.

Organism-specific databases

MaizeGDBi194080.

Phylogenomic databases

KOiK00279.

Enzyme and pathway databases

BioCyciMetaCyc:CKX1-MONOMER.
BRENDAi1.5.99.12. 6752.
SABIO-RKQ9T0N8.

Miscellaneous databases

EvolutionaryTraceiQ9T0N8.
PROiQ9T0N8.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProiIPR016169. 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]
PfamiPF09265. Cytokin-bind. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCKX1_MAIZE
AccessioniPrimary (citable) accession number: Q9T0N8
Secondary accession number(s): O81158
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: May 24, 2005
Last modified: November 2, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.