CKX1_ARATH
ID CKX1_ARATH Reviewed; 575 AA.
AC O22213;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cytokinin dehydrogenase 1;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 1;
DE Short=AtCKX1;
DE Short=CKO 1;
DE Flags: Precursor;
GN Name=CKX1; OrderedLocusNames=At2g41510; ORFNames=T32G6.3;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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.
RX PubMed=11504909; DOI=10.1073/pnas.171304098;
RA Werner T., Motyka V., Strnad M., Schmuelling T.;
RT "Regulation of plant growth by cytokinin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10487-10492(2001).
RN [5]
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 [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:0000269|PubMed:11504909,
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for isopentenyladenine {ECO:0000269|PubMed:14555694};
CC Vmax=0.1 nmol/h/mg enzyme {ECO:0000269|PubMed:14555694};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:14555694}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot apexes, lateral shoot meristems,
CC growing tissues of young flowers, and weakly at the root-hypocotyl
CC junction. {ECO:0000269|PubMed:14555694}.
CC -!- MISCELLANEOUS: The enzymatic activity is significantly greater under
CC acidic conditions in vitro.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK226615; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC002510; AAB84333.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09992.1; -; Genomic_DNA.
DR EMBL; AK226615; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T00807; T00807.
DR RefSeq; NP_001318403.1; NM_001336920.1.
DR AlphaFoldDB; O22213; -.
DR SMR; O22213; -.
DR STRING; 3702.AT2G41510.1; -.
DR iPTMnet; O22213; -.
DR PaxDb; O22213; -.
DR PRIDE; O22213; -.
DR ProteomicsDB; 222092; -.
DR EnsemblPlants; AT2G41510.1; AT2G41510.1; AT2G41510.
DR GeneID; 818749; -.
DR Gramene; AT2G41510.1; AT2G41510.1; AT2G41510.
DR KEGG; ath:AT2G41510; -.
DR Araport; AT2G41510; -.
DR TAIR; locus:2062714; AT2G41510.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024955_1_0_1; -.
DR InParanoid; O22213; -.
DR PhylomeDB; O22213; -.
DR BioCyc; MetaCyc:AT2G41510-MON; -.
DR BRENDA; 1.5.99.12; 399.
DR SABIO-RK; O22213; -.
DR PRO; PR:O22213; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22213; baseline and differential.
DR Genevisible; O22213; AT.
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:0009823; P:cytokinin catabolic process; IDA:TAIR.
DR GO; GO:0048507; P:meristem development; IMP: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 FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal; Vacuole.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..575
FT /note="Cytokinin dehydrogenase 1"
FT /id="PRO_0000020418"
FT DOMAIN 84..262
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 120..124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 125..126
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 197..201
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 533..536
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 125
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 411
FT /note="I -> V (in Ref. 3; AK226615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 64924 MW; 3005D391A6F4C192 CRC64;
MGLTSSLRFH RQNNKTFLGI FMILVLSCIP GRTNLCSNHS VSTPKELPSS NPSDIRSSLV
SLDLEGYISF DDVHNVAKDF GNRYQLPPLA ILHPRSVFDI SSMMKHIVHL GSTSNLTVAA
RGHGHSLQGQ ALAHQGVVIK MESLRSPDIR IYKGKQPYVD VSGGEIWINI LRETLKYGLS
PKSWTDYLHL TVGGTLSNAG ISGQAFKHGP QINNVYQLEI VTGKGEVVTC SEKRNSELFF
SVLGGLGQFG IITRARISLE PAPHMVKWIR VLYSDFSAFS RDQEYLISKE KTFDYVEGFV
IINRTDLLNN WRSSFSPNDS TQASRFKSDG KTLYCLEVVK YFNPEEASSM DQETGKLLSE
LNYIPSTLFS SEVPYIEFLD RVHIAERKLR AKGLWEVPHP WLNLLIPKSS IYQFATEVFN
NILTSNNNGP ILIYPVNQSK WKKHTSLITP NEDIFYLVAF LPSAVPNSSG KNDLEYLLKQ
NQRVMNFCAA ANLNVKQYLP HYETQKEWKS HFGKRWETFA QRKQAYDPLA ILAPGQRIFQ
KTTGKLSPIQ LAKSKATGSP QRYHYASILP KPRTV
