CKX2_ARATH
ID CKX2_ARATH Reviewed; 501 AA.
AC Q9FUJ3; Q9ZUP1;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cytokinin dehydrogenase 2;
DE EC=1.5.99.12 {ECO:0000269|PubMed:14555694};
DE AltName: Full=Cytokinin oxidase 2;
DE Short=AtCKX2;
DE Short=CKO 2;
DE Flags: Precursor;
GN Name=CKX2; OrderedLocusNames=At2g19500; ORFNames=F3P11.10;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
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: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 Evidence={ECO:0000269|PubMed:14555694};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 uM for isopentenyladenine {ECO:0000269|PubMed:14555694};
CC Vmax=7.4 nmol/h/mg enzyme {ECO:0000269|PubMed:14555694};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:14555694}. Secreted, extracellular space
CC {ECO:0000269|PubMed:14555694}.
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apex, in stipules, and
CC occasionally in the most apical part of the inflorescence stems. Not
CC detected in roots. {ECO:0000269|PubMed:14555694}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF303978; AAG30905.1; -; mRNA.
DR EMBL; AC005917; AAD10149.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06889.1; -; Genomic_DNA.
DR EMBL; BT004107; AAO42130.1; -; mRNA.
DR EMBL; BT005653; AAO64073.1; -; mRNA.
DR PIR; E84577; E84577.
DR RefSeq; NP_565455.1; NM_127508.2.
DR AlphaFoldDB; Q9FUJ3; -.
DR SMR; Q9FUJ3; -.
DR STRING; 3702.AT2G19500.1; -.
DR BindingDB; Q9FUJ3; -.
DR ChEMBL; CHEMBL6133; -.
DR PaxDb; Q9FUJ3; -.
DR PRIDE; Q9FUJ3; -.
DR ProteomicsDB; 222613; -.
DR EnsemblPlants; AT2G19500.1; AT2G19500.1; AT2G19500.
DR GeneID; 816469; -.
DR Gramene; AT2G19500.1; AT2G19500.1; AT2G19500.
DR KEGG; ath:AT2G19500; -.
DR Araport; AT2G19500; -.
DR TAIR; locus:2050349; AT2G19500.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024955_1_0_1; -.
DR InParanoid; Q9FUJ3; -.
DR OMA; RAKWFRM; -.
DR OrthoDB; 440623at2759; -.
DR PhylomeDB; Q9FUJ3; -.
DR BioCyc; ARA:AT2G19500-MON; -.
DR BioCyc; MetaCyc:AT2G19500-MON; -.
DR BRENDA; 1.5.99.12; 399.
DR SABIO-RK; Q9FUJ3; -.
DR PRO; PR:Q9FUJ3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9FUJ3; baseline and differential.
DR Genevisible; Q9FUJ3; AT.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:TAIR.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0019139; F:cytokinin dehydrogenase activity; IMP: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; 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 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; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..501
FT /note="Cytokinin dehydrogenase 2"
FT /id="PRO_0000020419"
FT DOMAIN 53..226
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 87..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 92..93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 161..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 495..498
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 92
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 157
FT /note="G -> R (in Ref. 1; AAG30905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 55583 MW; 9F8F0AAEAA4DE84A CRC64;
MANLRLMITL ITVLMITKSS NGIKIDLPKS LNLTLSTDPS IISAASHDFG NITTVTPGGV
ICPSSTADIS RLLQYAANGK STFQVAARGQ GHSLNGQASV SGGVIVNMTC ITDVVVSKDK
KYADVAAGTL WVDVLKKTAE KGVSPVSWTD YLHITVGGTL SNGGIGGQVF RNGPLVSNVL
ELDVITGKGE MLTCSRQLNP ELFYGVLGGL GQFGIITRAR IVLDHAPKRA KWFRMLYSDF
TTFTKDQERL ISMANDIGVD YLEGQIFLSN GVVDTSFFPP SDQSKVADLV KQHGIIYVLE
VAKYYDDPNL PIISKVIDTL TKTLSYLPGF ISMHDVAYFD FLNRVHVEEN KLRSLGLWEL
PHPWLNLYVP KSRILDFHNG VVKDILLKQK SASGLALLYP TNRNKWDNRM SAMIPEIDED
VIYIIGLLQS ATPKDLPEVE SVNEKIIRFC KDSGIKIKQY LMHYTSKEDW IEHFGSKWDD
FSKRKDLFDP KKLLSPGQDI F
