Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9T0N8

- CKX1_MAIZE

UniProt

Q9T0N8 - CKX1_MAIZE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cytokinin dehydrogenase 1

Gene

CKX1

Organism
Zea mays (Maize)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101FAD; via carbonyl oxygenBy similarity
Binding sitei169 – 1691FAD; via amide nitrogenBy similarity
Binding sitei174 – 1741FADBy similarity
Binding sitei235 – 2351FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei491 – 4911FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi100 – 1045FADBy similarity
Nucleotide bindingi105 – 1062FADBy similarity
Nucleotide bindingi180 – 1845FADBy similarity
Nucleotide bindingi527 – 5304FADBy similarity

GO - Molecular functioni

  1. cytokinin dehydrogenase activity Source: UniProtKB-EC
  2. flavin adenine dinucleotide binding Source: InterPro
  3. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro

GO - Biological processi

  1. cytokinin metabolic process Source: InterPro
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 cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiQ9T0N8.
MaizeGDBi194080.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 534516Cytokinin dehydrogenase 1PRO_0000020424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Modified residuei105 – 1051Pros-8alpha-FAD histidine
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi434 – 4341N-linked (GlcNAc...)Sequence Analysis

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

1
534
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni41 – 455Combined sources
Helixi51 – 566Combined sources
Beta strandi70 – 734Combined sources
Helixi78 – 9013Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi116 – 1205Combined sources
Helixi121 – 1255Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi139 – 1457Combined sources
Helixi150 – 1589Combined sources
Turni159 – 1613Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi169 – 1713Combined sources
Helixi175 – 1795Combined sources
Helixi188 – 1914Combined sources
Helixi194 – 1963Combined sources
Beta strandi197 – 2059Combined sources
Beta strandi210 – 2189Combined sources
Helixi219 – 2257Combined sources
Beta strandi232 – 24413Combined sources
Beta strandi247 – 25711Combined sources
Helixi259 – 27012Combined sources
Beta strandi285 – 2939Combined sources
Helixi294 – 2963Combined sources
Helixi297 – 3026Combined sources
Beta strandi305 – 3073Combined sources
Helixi309 – 32113Combined sources
Beta strandi325 – 33612Combined sources
Helixi345 – 35410Combined sources
Beta strandi364 – 3707Combined sources
Helixi371 – 3755Combined sources
Helixi377 – 38711Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi398 – 4036Combined sources
Helixi404 – 4063Combined sources
Helixi407 – 4148Combined sources
Turni415 – 4217Combined sources
Beta strandi428 – 4347Combined sources
Helixi435 – 4373Combined sources
Beta strandi448 – 45710Combined sources
Helixi466 – 48318Combined sources
Beta strandi489 – 4924Combined sources
Helixi498 – 5058Combined sources
Helixi507 – 52014Combined sources
Helixi528 – 5303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 32-534.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9T0N8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 245181FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi339 – 3457Poly-Ala

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791G → A in CAA77151. (PubMed:10230061)Curated
Sequence conflicti168 – 1681N → T in CAA77151. (PubMed:10230061)Curated
Sequence conflicti254 – 2541F → L in CAA77151. (PubMed:10230061)Curated

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 .
PIRi T01500.
T51929.
RefSeqi NP_001105591.1. NM_001112121.1.
UniGenei Zm.209.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W1O X-ray 1.70 A 1-534 [» ]
1W1Q X-ray 1.80 A 1-534 [» ]
1W1R X-ray 1.90 A 1-534 [» ]
1W1S X-ray 2.00 A 1-534 [» ]
2QKN X-ray 2.15 A 19-534 [» ]
2QPM X-ray 1.85 A 19-534 [» ]
3BW7 X-ray 1.95 A 19-534 [» ]
3C0P X-ray 1.95 A 19-534 [» ]
3DQ0 X-ray 1.90 A 19-534 [» ]
3KJM X-ray 1.90 A 19-534 [» ]
3S1C X-ray 2.09 A 19-534 [» ]
3S1D X-ray 1.75 A 19-534 [» ]
3S1E X-ray 1.90 A 19-534 [» ]
3S1F X-ray 2.00 A 19-534 [» ]
ProteinModelPortali Q9T0N8.
SMRi Q9T0N8. Positions 32-534.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL5363.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 542585.
KEGGi zma:542585.

Organism-specific databases

Gramenei Q9T0N8.
MaizeGDBi 194080.

Phylogenomic databases

KOi K00279.

Enzyme and pathway databases

BioCyci MetaCyc:CKX1-MONOMER.
BRENDAi 1.5.99.12. 6752.
SABIO-RK Q9T0N8.

Miscellaneous databases

EvolutionaryTracei Q9T0N8.

Family and domain databases

Gene3Di 3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProi IPR016169. 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 ]
Pfami PF09265. Cytokin-bind. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view ]
SUPFAMi SSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEi PS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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, IDENTIFICATION BY 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.

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 26, 2014
This is version 93 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, Direct protein sequencing

Documents

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

External Data

Dasty 3