CKX5_ARATH
ID CKX5_ARATH Reviewed; 540 AA.
AC Q67YU0; Q9FUJ0; Q9FWT3;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cytokinin dehydrogenase 5;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 5;
DE Short=AtCKX5;
DE Short=AtCKX6;
DE Short=CKO5;
DE Flags: Precursor;
GN Name=CKX5; Synonyms=CKX6; OrderedLocusNames=At1g75450; ORFNames=F1B16.2;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q67YU0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the developing leaf petioles and in
CC the rib zone of the axillary shoot meristems. In roots, expressed in
CC the vascular cylinder within the root apical meristem and only faintly
CC detectable in the differentiated root. {ECO:0000269|PubMed:14555694}.
CC -!- DEVELOPMENTAL STAGE: Expressed in young developing stamen primordia and
CC later confined to the central part of growing anthers. Before and
CC during pollination, restricted to the maturing pollen grains.
CC {ECO:0000269|PubMed:14555694}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG13068.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF303982; AAG30909.1; -; mRNA.
DR EMBL; AC023754; AAG13068.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35721.1; -; Genomic_DNA.
DR EMBL; AK176378; BAD44141.1; -; mRNA.
DR PIR; B96785; B96785.
DR RefSeq; NP_177678.2; NM_106199.5. [Q67YU0-1]
DR AlphaFoldDB; Q67YU0; -.
DR SMR; Q67YU0; -.
DR STRING; 3702.AT1G75450.1; -.
DR PaxDb; Q67YU0; -.
DR PRIDE; Q67YU0; -.
DR ProteomicsDB; 222094; -. [Q67YU0-1]
DR EnsemblPlants; AT1G75450.1; AT1G75450.1; AT1G75450. [Q67YU0-1]
DR GeneID; 843881; -.
DR Gramene; AT1G75450.1; AT1G75450.1; AT1G75450. [Q67YU0-1]
DR KEGG; ath:AT1G75450; -.
DR Araport; AT1G75450; -.
DR TAIR; locus:2018437; AT1G75450.
DR eggNOG; KOG1231; Eukaryota.
DR InParanoid; Q67YU0; -.
DR OrthoDB; 733611at2759; -.
DR PhylomeDB; Q67YU0; -.
DR BioCyc; ARA:AT1G75450-MON; -.
DR PRO; PR:Q67YU0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q67YU0; baseline and differential.
DR Genevisible; Q67YU0; AT.
DR GO; GO:0005576; C:extracellular region; TAS:TAIR.
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: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 2: Evidence at transcript level;
KW Alternative splicing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..540
FT /note="Cytokinin dehydrogenase 5"
FT /id="PRO_0000020422"
FT DOMAIN 63..241
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 97..101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 102..103
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 176..180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 514..517
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 185
FT /note="F -> L (in Ref. 1; AAG30909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 60424 MW; 9B3BA11386252B84 CRC64;
MNREMTSSFL LLTFAICKLI IAVGLNVGPS ELLRIGAIDV DGHFTVHPSD LASVSSDFGM
LKSPEEPLAV LHPSSAEDVA RLVRTAYGSA TAFPVSARGH GHSINGQAAA GRNGVVVEMN
HGVTGTPKPL VRPDEMYVDV WGGELWVDVL KKTLEHGLAP KSWTDYLYLT VGGTLSNAGI
SGQAFHHGPQ ISNVLELDVV TGKGEVMRCS EEENTRLFHG VLGGLGQFGI ITRARISLEP
APQRVRWIRV LYSSFKVFTE DQEYLISMHG QLKFDYVEGF VIVDEGLVNN WRSSFFSPRN
PVKISSVSSN GSVLYCLEIT KNYHDSDSEI VDQEVEILMK KLNFIPTSVF TTDLQYVDFL
DRVHKAELKL RSKNLWEVPH PWLNLFVPKS RISDFDKGVF KGILGNKTSG PILIYPMNKD
KWDERSSAVT PDEEVFYLVA LLRSALTDGE ETQKLEYLKD QNRRILEFCE QAKINVKQYL
PHHATQEEWV AHFGDKWDRF RSLKAEFDPR HILATGQRIF QNPSLSLFPP SSSSSSAASW
