CKX5_ORYSJ
ID CKX5_ORYSJ Reviewed; 534 AA.
AC Q5ZAY9; A0A0P0V8U9;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cytokinin dehydrogenase 5;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 5;
DE Short=OsCKX5;
DE Flags: Precursor;
GN Name=CKX5; OrderedLocusNames=Os01g0775400, LOC_Os01g56810;
GN ORFNames=P0413G02.1, P0490D09.33;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP REVIEW.
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 [7]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Koshihikari;
RX PubMed=15976269; DOI=10.1126/science.1113373;
RA Ashikari M., Sakakibara H., Lin S., Yamamoto T., Takashi T., Nishimura A.,
RA Angeles E.R., Qian Q., Kitano H., Matsuoka M.;
RT "Cytokinin oxidase regulates rice grain production.";
RL Science 309:741-745(2005).
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; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescence meristems.
CC {ECO:0000269|PubMed:15976269}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AP003265; BAD52957.1; -; Genomic_DNA.
DR EMBL; AP003344; BAD53232.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF06323.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS74596.1; -; Genomic_DNA.
DR EMBL; AK101022; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015625924.1; XM_015770438.1.
DR AlphaFoldDB; Q5ZAY9; -.
DR SMR; Q5ZAY9; -.
DR STRING; 4530.OS01T0775400-01; -.
DR PaxDb; Q5ZAY9; -.
DR PRIDE; Q5ZAY9; -.
DR EnsemblPlants; Os01t0775400-01; Os01t0775400-01; Os01g0775400.
DR GeneID; 4327887; -.
DR Gramene; Os01t0775400-01; Os01t0775400-01; Os01g0775400.
DR KEGG; osa:4327887; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024955_1_0_1; -.
DR InParanoid; Q5ZAY9; -.
DR OMA; ITFAICR; -.
DR OrthoDB; 733611at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5ZAY9; OS.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0019139; F:cytokinin dehydrogenase activity; IC:Gramene.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009690; P:cytokinin metabolic process; IEA:InterPro.
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 FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..534
FT /note="Cytokinin dehydrogenase 5"
FT /id="PRO_0000394208"
FT DOMAIN 59..243
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 93..97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 98..99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 103
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 484
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 519..522
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 156
FT /note="A -> E (in Ref. 5; AK101022)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="H -> N (in Ref. 5; AK101022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 58202 MW; 8B8DBB167F69F181 CRC64;
MAWCLVFMVF LIYCLISTVG LPVAPADEAA MQLGGVGGGR LSVEPSDVME ASLDFGRLTS
AEPLAVFHPR GAGDVAALVK AAYGSASGIR VSARGHGHSI SGQAQAAGGV VVDMSHGWRA
EAAERTLPVY SPALGGHYID VWGGELWIDV LNWTLAHGGL APRSWTDYLY LSVGGTLSNA
GISGQAFHHG PQISNVYELD VVTGKGEVVT CSESNNPDLF FGALGGLGQL GIITRARIAL
EPAPHRVRWI RALYSNFTEF TADQERLISL QHGGRRFDYV EGFVVAAEGL INNWRSSFFS
PQNPVKLSSL KHHSGVLYCL EVTKNYDDST AVTVDQDVEA LLGELNFIPG TVFTTDLPYV
DFLDRVHKAE LKLRGKGMWE VPHPWLNLFV PASRIADFDR GVFRGVLGSR TAGGPILIYP
MNRHKWDPRS SVVTPEEDVF YLVAFLRSAV PGSTDPAQSL EALERQNREI LEFCDEAGIG
AKQYLPNHKA QREWEAHFGA RWARFARLKA EFDPRAMLAT GQGIFDSPPL LAES
