CKX3_ARATH
ID CKX3_ARATH Reviewed; 523 AA.
AC Q9LTS3;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cytokinin dehydrogenase 3;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 3;
DE Short=AtCKX3;
DE Short=CKO 3;
DE Flags: Precursor;
GN Name=CKX3; OrderedLocusNames=At5g56970; ORFNames=MHM17.8;
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 [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP 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 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).
RN [6]
RP INDUCTION BY GATA18/HAN, AND TISSUE SPECIFICITY.
RX PubMed=26390296; DOI=10.1371/journal.pgen.1005479;
RA Ding L., Yan S., Jiang L., Zhao W., Ning K., Zhao J., Liu X., Zhang J.,
RA Wang Q., Zhang X.;
RT "HANABA TARANU (HAN) bridges meristem and organ primordia boundaries
RT through PINHEAD, JAGGED, BLADE-ON-PETIOLE2 and CYTOKININ OXIDASE 3 during
RT flower development in Arabidopsis.";
RL PLoS Genet. 11:E1005479-E1005479(2015).
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: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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.2 uM for isopentenyladenine {ECO:0000269|PubMed:14555694};
CC Vmax=7.7 nmol/h/mg enzyme {ECO:0000269|PubMed:14555694};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:14555694}. Vacuole {ECO:0000269|PubMed:14555694}.
CC -!- TISSUE SPECIFICITY: Very weak expression in the young shoot tissues
CC around two weeks after germination (PubMed:14555694). Present in the
CC center of the floral meristem and the boundary between long stamen
CC primordia and gynoecial primordia (PubMed:26390296).
CC {ECO:0000269|PubMed:14555694, ECO:0000269|PubMed:26390296}.
CC -!- INDUCTION: Regulated by GATA18/HAN. {ECO:0000269|PubMed:26390296}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF303979; AAG30906.1; -; mRNA.
DR EMBL; AB024035; BAA97027.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96828.1; -; Genomic_DNA.
DR RefSeq; NP_200507.1; NM_125079.3.
DR AlphaFoldDB; Q9LTS3; -.
DR SMR; Q9LTS3; -.
DR BioGRID; 21043; 2.
DR STRING; 3702.AT5G56970.1; -.
DR iPTMnet; Q9LTS3; -.
DR PaxDb; Q9LTS3; -.
DR PRIDE; Q9LTS3; -.
DR ProteomicsDB; 222614; -.
DR EnsemblPlants; AT5G56970.1; AT5G56970.1; AT5G56970.
DR GeneID; 835799; -.
DR Gramene; AT5G56970.1; AT5G56970.1; AT5G56970.
DR KEGG; ath:AT5G56970; -.
DR Araport; AT5G56970; -.
DR TAIR; locus:2164615; AT5G56970.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024955_1_0_1; -.
DR InParanoid; Q9LTS3; -.
DR OrthoDB; 350817at2759; -.
DR PhylomeDB; Q9LTS3; -.
DR BioCyc; ARA:AT5G56970-MON; -.
DR BioCyc; MetaCyc:AT5G56970-MON; -.
DR BRENDA; 1.5.99.12; 399.
DR SABIO-RK; Q9LTS3; -.
DR PRO; PR:Q9LTS3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTS3; baseline and differential.
DR Genevisible; Q9LTS3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0019139; F:cytokinin dehydrogenase activity; IDA:TAIR.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:TAIR.
DR GO; GO:0009823; P:cytokinin catabolic process; IDA: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 InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
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.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Reference proteome; Signal; Vacuole.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..523
FT /note="Cytokinin dehydrogenase 3"
FT /id="PRO_0000020420"
FT DOMAIN 66..243
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 100..104
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 105..106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 167
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 178..182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 511..514
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 523 AA; 59423 MW; 2324EBFC21D7103A CRC64;
MASYNLRSQV RLIAITIVII ITLSTPITTN TSPQPWNILS HNEFAGKLTS SSSSVESAAT
DFGHVTKIFP SAVLIPSSVE DITDLIKLSF DSQLSFPLAA RGHGHSHRGQ ASAKDGVVVN
MRSMVNRDRG IKVSRTCLYV DVDAAWLWIE VLNKTLELGL TPVSWTDYLY LTVGGTLSNG
GISGQTFRYG PQITNVLEMD VITGKGEIAT CSKDMNSDLF FAVLGGLGQF GIITRARIKL
EVAPKRAKWL RFLYIDFSEF TRDQERVISK TDGVDFLEGS IMVDHGPPDN WRSTYYPPSD
HLRIASMVKR HRVIYCLEVV KYYDETSQYT VNEEMEELSD SLNHVRGFMY EKDVTYMDFL
NRVRTGELNL KSKGQWDVPH PWLNLFVPKT QISKFDDGVF KGIILRNNIT SGPVLVYPMN
RNKWNDRMSA AIPEEDVFYA VGFLRSAGFD NWEAFDQENM EILKFCEDAN MGVIQYLPYH
SSQEGWVRHF GPRWNIFVER KYKYDPKMIL SPGQNIFQKI NSS
