CKX7_ARATH
ID CKX7_ARATH Reviewed; 524 AA.
AC Q9FUJ1;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cytokinin dehydrogenase 7;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 7;
DE Short=AtCKX5;
DE Short=AtCKX7;
DE Short=CKO7;
GN Name=CKX7; Synonyms=CKX5; OrderedLocusNames=At5g21482; ORFNames=F13M11;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-524 IN COMPLEX WITH FAD.
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-524.
RG Center for eukaryotic structural genomics (CESG);
RT "X-ray structure of cytokinin oxidase/dehydrogenase (CKX) from Arabidopsis
RT thaliana At5g21482.";
RL Submitted (NOV-2005) to the PDB data bank.
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 -!- 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;
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF303981; AAG30908.1; -; mRNA.
DR EMBL; AC140977; AAO73882.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92951.1; -; Genomic_DNA.
DR RefSeq; NP_850863.1; NM_180532.3.
DR PDB; 2EXR; X-ray; 1.70 A; A=2-524.
DR PDB; 2Q4W; X-ray; 1.70 A; A=2-524.
DR PDBsum; 2EXR; -.
DR PDBsum; 2Q4W; -.
DR AlphaFoldDB; Q9FUJ1; -.
DR SMR; Q9FUJ1; -.
DR STRING; 3702.AT5G21482.1; -.
DR PaxDb; Q9FUJ1; -.
DR PRIDE; Q9FUJ1; -.
DR ProteomicsDB; 222095; -.
DR DNASU; 832248; -.
DR EnsemblPlants; AT5G21482.1; AT5G21482.1; AT5G21482.
DR GeneID; 832248; -.
DR Gramene; AT5G21482.1; AT5G21482.1; AT5G21482.
DR KEGG; ath:AT5G21482; -.
DR Araport; AT5G21482; -.
DR TAIR; locus:1005716173; AT5G21482.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024955_1_0_1; -.
DR InParanoid; Q9FUJ1; -.
DR OMA; YDYKIYF; -.
DR OrthoDB; 350817at2759; -.
DR PhylomeDB; Q9FUJ1; -.
DR BioCyc; ARA:AT5G21482-MON; -.
DR BRENDA; 1.5.99.12; 399.
DR EvolutionaryTrace; Q9FUJ1; -.
DR PRO; PR:Q9FUJ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FUJ1; baseline and differential.
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 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 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..524
FT /note="Cytokinin dehydrogenase 7"
FT /id="PRO_0000128156"
FT DOMAIN 58..238
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 91..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT BINDING 96..97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT BINDING 101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT BINDING 167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT BINDING 173..177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT BINDING 479
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT BINDING 514..517
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17850744"
FT MOD_RES 96
FT /note="Pros-8alpha-FAD histidine"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2EXR"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2EXR"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 224..237
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 252..263
FT /evidence="ECO:0007829|PDB:2Q4W"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:2Q4W"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 311..322
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 356..360
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 389..398
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 399..403
FT /evidence="ECO:0007829|PDB:2Q4W"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 435..442
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 452..471
FT /evidence="ECO:0007829|PDB:2Q4W"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 486..493
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 497..507
FT /evidence="ECO:0007829|PDB:2Q4W"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:2Q4W"
SQ SEQUENCE 524 AA; 57976 MW; 9ADB3BE97A7F063C CRC64;
MIAYIEPYFL ENDAEAASAA TAAGKSTDGV SESLNIQGEI LCGGAAADIA GRDFGGMNCV
KPLAVVRPVG PEDIAGAVKA ALRSDKLTVA ARGNGHSING QAMAEGGLVV DMSTTAENHF
EVGYLSGGDA TAFVDVSGGA LWEDVLKRCV SEYGLAPRSW TDYLGLTVGG TLSNAGVSGQ
AFRYGPQTSN VTELDVVTGN GDVVTCSEIE NSELFFSVLG GLGQFGIITR ARVLLQPAPD
MVRWIRVVYT EFDEFTQDAE WLVSQKNESS FDYVEGFVFV NGADPVNGWP TVPLHPDHEF
DPTRLPQSCG SVLYCLELGL HYRDSDSNST IDKRVERLIG RLRFNEGLRF EVDLPYVDFL
LRVKRSEEIA KENGTWETPH PWLNLFVSKR DIGDFNRTVF KELVKNGVNG PMLVYPLLRS
RWDDRTSVVI PEEGEIFYIV ALLRFVPPCA KVSSVEKMVA QNQEIVHWCV KNGIDYKLYL
PHYKSQEEWI RHFGNRWSRF VDRKAMFDPM AILSPGQKIF NRSL
