CKX11_ORYSJ
ID CKX11_ORYSJ Reviewed; 518 AA.
AC Q6Z955;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytokinin dehydrogenase 11;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 11;
DE Short=OsCKX11;
DE Flags: Precursor;
GN Name=CKX11; OrderedLocusNames=Os08g0460600, LOC_Os08g35860;
GN ORFNames=P0690E03.23;
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=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 [2]
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 [3]
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; AP004707; BAD09964.1; -; Genomic_DNA.
DR EMBL; AP014964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015650661.1; XM_015795175.1.
DR AlphaFoldDB; Q6Z955; -.
DR SMR; Q6Z955; -.
DR STRING; 4530.OS08T0460600-01; -.
DR PaxDb; Q6Z955; -.
DR PRIDE; Q6Z955; -.
DR GeneID; 4345764; -.
DR KEGG; osa:4345764; -.
DR eggNOG; KOG1231; Eukaryota.
DR InParanoid; Q6Z955; -.
DR OrthoDB; 350817at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0019139; F:cytokinin dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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 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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..518
FT /note="Cytokinin dehydrogenase 11"
FT /id="PRO_0000394215"
FT DOMAIN 41..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 74..78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 79..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 153..157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 497..500
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 79
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 55341 MW; B0E3556A47D260A5 CRC64;
MMLAYMDHAA AAAEPDAGAE PAVAAVDAAE FAAAMDFGGL VSARPAAVVR PASSDDVASA
IRAAARTAHL TVAARGNGHS VAGQAMARGG LVLDMRALPR RMQLVVAPSG EKFADVPGGA
LWEEVLHWAV SKHGLAPASW TDYLRLTVGG TLSNGGVSGQ SFRYGPQVSN VAQLEVVTGD
GECHVCSRSA DPDLFFAVLG GLGQFGVITR ARIPLSPAPQ TVRWTRVVYA SFADYAADAE
WLVTRPPHEA FDYVEGFAFV RSDDPVNGWP TVPIPDGAHF DASLLPANAG PVLYCLEVAL
YQRGGGGDGG GDDMDKRVGE MMRQLKYVRG LEFAAGVGYV DFLSRVNRVE DEARRNGSWA
APHPWLNLFI SSRDIAAFDR AVLNGMLADG VDGPMLIYPM LKSKWDPATS VALPNGEIFY
LVALLRFCRP YPGGGPPVDE LVAQNNAIID ACRSNGYDYK IYFPSYHAQS DWSRHFGAKW
SRFVDRKARY DPLAILAPGQ NIFARTPSSV AAAAAVIV
