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Protein

Cytokinin dehydrogenase 7

Gene

CKX7

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011FAD; via carbonyl oxygen1 Publication
Binding sitei162 – 1621FAD; via amide nitrogen1 Publication
Binding sitei167 – 1671FAD1 Publication
Binding sitei228 – 2281FAD; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei479 – 4791FAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi91 – 955FAD1 Publication
Nucleotide bindingi96 – 972FAD1 Publication
Nucleotide bindingi173 – 1775FAD1 Publication
Nucleotide bindingi514 – 5174FAD1 Publication

GO - Molecular functioni

GO - Biological processi

  • cytokinin catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciARA:AT5G21482-MONOMER.
BRENDAi1.5.99.12. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytokinin dehydrogenase 7 (EC:1.5.99.12)
Alternative name(s):
Cytokinin oxidase 7
Short name:
AtCKX5
Short name:
AtCKX7
Short name:
CKO7
Gene namesi
Name:CKX7
Synonyms:CKX5
Ordered Locus Names:At5g21482
ORF Names:F13M11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G21482.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Cytokinin dehydrogenase 7PRO_0000128156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961Pros-8alpha-FAD histidine

Proteomic databases

PaxDbiQ9FUJ1.
PRIDEiQ9FUJ1.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G21482.1.

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 415Combined sources
Helixi44 – 496Combined sources
Beta strandi63 – 664Combined sources
Helixi71 – 8313Combined sources
Beta strandi84 – 863Combined sources
Beta strandi89 – 957Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi107 – 1115Combined sources
Helixi112 – 1187Combined sources
Beta strandi120 – 1245Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi132 – 1376Combined sources
Helixi142 – 15312Combined sources
Beta strandi154 – 1563Combined sources
Beta strandi165 – 1673Combined sources
Helixi168 – 1725Combined sources
Helixi181 – 1844Combined sources
Helixi187 – 1904Combined sources
Beta strandi191 – 1988Combined sources
Beta strandi203 – 2064Combined sources
Helixi212 – 2187Combined sources
Beta strandi224 – 23714Combined sources
Beta strandi240 – 25011Combined sources
Helixi252 – 26312Combined sources
Turni267 – 2693Combined sources
Beta strandi272 – 2765Combined sources
Beta strandi279 – 2824Combined sources
Turni285 – 2873Combined sources
Helixi289 – 2913Combined sources
Helixi302 – 3043Combined sources
Beta strandi311 – 32212Combined sources
Helixi328 – 33912Combined sources
Beta strandi349 – 3557Combined sources
Helixi356 – 3605Combined sources
Helixi363 – 37311Combined sources
Beta strandi376 – 3783Combined sources
Beta strandi383 – 3886Combined sources
Helixi389 – 39810Combined sources
Helixi399 – 4035Combined sources
Turni404 – 4063Combined sources
Beta strandi412 – 4187Combined sources
Helixi419 – 4213Combined sources
Beta strandi435 – 4428Combined sources
Helixi452 – 47120Combined sources
Beta strandi476 – 4805Combined sources
Helixi486 – 4938Combined sources
Helixi494 – 4963Combined sources
Helixi497 – 50711Combined sources
Helixi515 – 5173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EXRX-ray1.70A2-524[»]
2Q4WX-ray1.70A2-524[»]
ProteinModelPortaliQ9FUJ1.
SMRiQ9FUJ1. Positions 34-524.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9FUJ1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 238181FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1231. Eukaryota.
COG0277. LUCA.
HOGENOMiHOG000237593.
InParanoidiQ9FUJ1.
KOiK00279.
OMAiVRWTRVV.
PhylomeDBiQ9FUJ1.

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.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FUJ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAYIEPYFL ENDAEAASAA TAAGKSTDGV SESLNIQGEI LCGGAAADIA
60 70 80 90 100
GRDFGGMNCV KPLAVVRPVG PEDIAGAVKA ALRSDKLTVA ARGNGHSING
110 120 130 140 150
QAMAEGGLVV DMSTTAENHF EVGYLSGGDA TAFVDVSGGA LWEDVLKRCV
160 170 180 190 200
SEYGLAPRSW TDYLGLTVGG TLSNAGVSGQ AFRYGPQTSN VTELDVVTGN
210 220 230 240 250
GDVVTCSEIE NSELFFSVLG GLGQFGIITR ARVLLQPAPD MVRWIRVVYT
260 270 280 290 300
EFDEFTQDAE WLVSQKNESS FDYVEGFVFV NGADPVNGWP TVPLHPDHEF
310 320 330 340 350
DPTRLPQSCG SVLYCLELGL HYRDSDSNST IDKRVERLIG RLRFNEGLRF
360 370 380 390 400
EVDLPYVDFL LRVKRSEEIA KENGTWETPH PWLNLFVSKR DIGDFNRTVF
410 420 430 440 450
KELVKNGVNG PMLVYPLLRS RWDDRTSVVI PEEGEIFYIV ALLRFVPPCA
460 470 480 490 500
KVSSVEKMVA QNQEIVHWCV KNGIDYKLYL PHYKSQEEWI RHFGNRWSRF
510 520
VDRKAMFDPM AILSPGQKIF NRSL
Length:524
Mass (Da):57,976
Last modified:March 1, 2001 - v1
Checksum:i9ADB3BE97A7F063C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF303981 mRNA. Translation: AAG30908.1.
AC140977 Genomic DNA. Translation: AAO73882.1.
CP002688 Genomic DNA. Translation: AED92951.1.
RefSeqiNP_850863.1. NM_180532.2.
UniGeneiAt.16886.

Genome annotation databases

EnsemblPlantsiAT5G21482.1; AT5G21482.1; AT5G21482.
GeneIDi832248.
GrameneiAT5G21482.1; AT5G21482.1; AT5G21482.
KEGGiath:AT5G21482.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF303981 mRNA. Translation: AAG30908.1.
AC140977 Genomic DNA. Translation: AAO73882.1.
CP002688 Genomic DNA. Translation: AED92951.1.
RefSeqiNP_850863.1. NM_180532.2.
UniGeneiAt.16886.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EXRX-ray1.70A2-524[»]
2Q4WX-ray1.70A2-524[»]
ProteinModelPortaliQ9FUJ1.
SMRiQ9FUJ1. Positions 34-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G21482.1.

Proteomic databases

PaxDbiQ9FUJ1.
PRIDEiQ9FUJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G21482.1; AT5G21482.1; AT5G21482.
GeneIDi832248.
GrameneiAT5G21482.1; AT5G21482.1; AT5G21482.
KEGGiath:AT5G21482.

Organism-specific databases

TAIRiAT5G21482.

Phylogenomic databases

eggNOGiKOG1231. Eukaryota.
COG0277. LUCA.
HOGENOMiHOG000237593.
InParanoidiQ9FUJ1.
KOiK00279.
OMAiVRWTRVV.
PhylomeDBiQ9FUJ1.

Enzyme and pathway databases

BioCyciARA:AT5G21482-MONOMER.
BRENDAi1.5.99.12. 399.

Miscellaneous databases

EvolutionaryTraceiQ9FUJ1.
PROiQ9FUJ1.

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.
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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  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. "Ensemble refinement of protein crystal structures: validation and application."
    Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.
    Structure 15:1040-1052(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-524 IN COMPLEX WITH FAD.
  6. "X-ray structure of cytokinin oxidase/dehydrogenase (CKX) from Arabidopsis thaliana At5g21482."
    Center for eukaryotic structural genomics (CESG)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-524.

Entry informationi

Entry nameiCKX7_ARATH
AccessioniPrimary (citable) accession number: Q9FUJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: March 1, 2001
Last modified: March 16, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.