CKX6_ARATH
ID CKX6_ARATH Reviewed; 533 AA.
AC Q9LY71; Q0WR65;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cytokinin dehydrogenase 6;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 6;
DE Short=AtCKX6;
DE Short=AtCKX7;
DE Short=CKO6;
DE Flags: Precursor;
GN Name=CKX6; Synonyms=CKX7; OrderedLocusNames=At3g63440; ORFNames=MAA21_70;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=14555694; DOI=10.1105/tpc.014928;
RA Werner T., Motyka V., Laucou V., Smets R., Van Onckelen H., Schmulling T.;
RT "Cytokinin-deficient transgenic Arabidopsis plants show multiple
RT developmental alterations indicating opposite functions of cytokinins in
RT the regulation of shoot and root meristem activity.";
RL Plant Cell 15:2532-2550(2003).
RN [5]
RP IDENTIFICATION.
RX PubMed=11154345; DOI=10.1104/pp.125.1.378;
RA Bilyeu K.D., Cole J.L., Laskey J.G., Riekhof W.R., Esparza T.J.,
RA Kramer M.D., Morris R.O.;
RT "Molecular and biochemical characterization of a cytokinin oxidase from
RT maize.";
RL Plant Physiol. 125:378-386(2001).
RN [6]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=12721786; DOI=10.1007/s10265-003-0096-4;
RA Schmuelling T., Werner T., Riefler M., Krupkova E., Bartrina y Manns I.;
RT "Structure and function of cytokinin oxidase/dehydrogenase genes of maize,
RT rice, Arabidopsis and other species.";
RL J. Plant Res. 116:241-252(2003).
CC -!- FUNCTION: Catalyzes the oxidation of cytokinins, a family of N(6)-
CC substituted adenine derivatives that are plant hormones, where the
CC substituent is an isopentenyl group. {ECO:0000250,
CC ECO:0000269|PubMed:14555694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + H2O + N(6)-dimethylallyladenine = 3-methyl-2-butenal +
CC adenine + AH2; Xref=Rhea:RHEA:13625, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15825, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:17660; EC=1.5.99.12;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular system of roots, of young
CC growing leaves and of the most apical portion of the growing stem. No
CC expression in the root apical meristem. In flowers, restricted to the
CC vascular bundles and transmitting tissue of developing gynoeciae.
CC {ECO:0000269|PubMed:14555694}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the maturation phase of stomatal
CC guard cells but not in fully mature stomata. In the root vasculature,
CC detected soon after germination, with a maxima around the lateral root
CC primordia. {ECO:0000269|PubMed:14555694}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF00384.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB87797.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163818; CAB87797.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80482.1; -; Genomic_DNA.
DR EMBL; AK228457; BAF00384.1; ALT_INIT; mRNA.
DR PIR; T49185; T49185.
DR RefSeq; NP_191903.3; NM_116209.3.
DR AlphaFoldDB; Q9LY71; -.
DR SMR; Q9LY71; -.
DR STRING; 3702.AT3G63440.1; -.
DR PaxDb; Q9LY71; -.
DR PRIDE; Q9LY71; -.
DR EnsemblPlants; AT3G63440.1; AT3G63440.1; AT3G63440.
DR GeneID; 825519; -.
DR Gramene; AT3G63440.1; AT3G63440.1; AT3G63440.
DR KEGG; ath:AT3G63440; -.
DR Araport; AT3G63440; -.
DR TAIR; locus:2087423; AT3G63440.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024955_1_0_1; -.
DR InParanoid; Q9LY71; -.
DR OMA; QKPIAYS; -.
DR OrthoDB; 733611at2759; -.
DR PhylomeDB; Q9LY71; -.
DR PRO; PR:Q9LY71; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY71; baseline and differential.
DR Genevisible; Q9LY71; AT.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0019139; F:cytokinin dehydrogenase activity; TAS:TAIR.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009690; P:cytokinin metabolic process; IEA:InterPro.
DR GO; GO:0010103; P:stomatal complex morphogenesis; TAS:TAIR.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; -; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR015345; Cytokinin_DH_FAD/cytokin-bd.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF09265; Cytokin-bind; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..533
FT /note="Cytokinin dehydrogenase 6"
FT /id="PRO_0000020423"
FT DOMAIN 68..248
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 104..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 109..110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 183..187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 520..523
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 533 AA; 60000 MW; C22B8682468048B9 CRC64;
MSYLHASLLR KRTMLIVRSF TILLLSCIAF KLACCFSSSI SSLKALPLVG HLEFEHVHHA
SKDFGNRYQL IPLAVLHPKS VSDIASTIRH IWMMGTHSQL TVAARGRGHS LQGQAQTRHG
IVIHMESLHP QKLQVYSVDS PAPYVDVSGG ELWINILHET LKYGLAPKSW TDYLHLTVGG
TLSNAGISGQ AFRHGPQISN VHQLEIVTGK GEILNCTKRQ NSDLFNGVLG GLGQFGIITR
ARIALEPAPT MVKWIRVLYL DFAAFAKDQE QLISAQGHKF DYIEGFVIIN RTGLLNSWRL
SFTAEEPLEA SQFKFDGRTL YCLELAKYLK QDNKDVINQE VKETLSELSY VTSTLFTTEV
AYEAFLDRVH VSEVKLRSKG QWEVPHPWLN LLVPRSKINE FARGVFGNIL TDTSNGPVIV
YPVNKSKWDN QTSAVTPEEE VFYLVAILTS ASPGSAGKDG VEEILRRNRR ILEFSEEAGI
GLKQYLPHYT TREEWRSHFG DKWGEFVRRK SRYDPLAILA PGHRIFQKAV SYS
