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Q9T0N8

- CKX1_MAIZE

UniProt

Q9T0N8 - CKX1_MAIZE

Protein

Cytokinin dehydrogenase 1

Gene

CKX1

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (24 May 2005)
      Previous versions | rss
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    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

    FAD.

    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

    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 space Source: UniProtKB-SubCell

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

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    MAVVYYLLLA GLIACSHALA AGTPALGDDR GRPWPASLAA LALDGKLRTD    50
    SNATAAASTD FGNITSALPA AVLYPSSTGD LVALLSAANS TPGWPYTIAF 100
    RGRGHSLMGQ AFAPGGVVVN MASLGDAAAP PRINVSADGR YVDAGGEQVW 150
    IDVLRASLAR GVAPRSWNDY LYLTVGGTLS NAGISGQAFR HGPQISNVLE 200
    MDVITGHGEM VTCSKQLNAD LFDAVLGGLG QFGVITRARI AVEPAPARAR 250
    WVRFVYTDFA AFSADQERLT APRPGGGGAS FGPMSYVEGS VFVNQSLATD 300
    LANTGFFTDA DVARIVALAG ERNATTVYSI EATLNYDNAT AAAAAVDQEL 350
    ASVLGTLSYV EGFAFQRDVA YAAFLDRVHG EEVALNKLGL WRVPHPWLNM 400
    FVPRSRIADF DRGVFKGILQ GTDIVGPLIV YPLNKSMWDD GMSAATPSED 450
    VFYAVSLLFS SVAPNDLARL QEQNRRILRF CDLAGIQYKT YLARHTDRSD 500
    WVRHFGAAKW NRFVEMKNKY DPKRLLSPGQ DIFN 534
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 91 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