ID   CKX10_ORYSJ             Reviewed;         550 AA.
AC   Q5Z620;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cytokinin dehydrogenase 10;
DE            EC=1.5.99.12;
DE   AltName: Full=Cytokinin oxidase 10;
DE            Short=OsCKX10;
DE   Flags: Precursor;
GN   Name=CKX10; OrderedLocusNames=Os06g0572300, LOC_Os06g37500;
GN   ORFNames=OSJNBa0006A22.17, P0610D01.25;
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   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   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AP004729; BAD61835.1; -; Genomic_DNA.
DR   EMBL; AP005460; BAD61939.1; -; Genomic_DNA.
DR   EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q5Z620; -.
DR   SMR; Q5Z620; -.
DR   STRING; 4530.OS06T0572300-00; -.
DR   PaxDb; Q5Z620; -.
DR   PRIDE; Q5Z620; -.
DR   eggNOG; KOG1231; Eukaryota.
DR   InParanoid; Q5Z620; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
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: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   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   3: Inferred from homology;
KW   FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..550
FT                   /note="Cytokinin dehydrogenase 10"
FT                   /id="PRO_0000394214"
FT   DOMAIN          64..245
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   REGION          523..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..550
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         98..102
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         103..104
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..184
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         489
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         524..527
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         103
FT                   /note="Pros-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   550 AA;  59921 MW;  E1381BDDBA866EAB CRC64;
     MMPRAQLTTF LIVTSFLSTV PYLRAPVHGG VLTSYDVSSL DIMSKIHTDH DATTKASSDF
     GHIVHATPNG VFRPTFPADI AALIRLSLSQ PTPFTVAPRG KGHSSRGQAF APGGIVVDMS
     ALGDHGHHTS HRIDVSVDRM YVDAGGEQLW IDVLHTALKH GLTPRVWTDY LRITVGGTLS
     NAGIGGQAFR HGPQISNVHE LDVVTGMGEM ITCSPEVNSA LFFAVLGGLG QFGVITRARI
     RLEPAPKRVK WVRIAYSDVH PFTTDQELLI SKWASGSGFD YVEGQVQLNR TLTQGRRSSS
     FFSATDLARL TGLAIDTGSV AIYYIEGAMY YDDNTAASVD QKLDALLEEL SFVRGFVFVR
     DASYVEFLDR VGREEQNLRS AGAWDVPHPW LNLFVPRSRI LHFDAAVFKG ILRNANPVGL
     ILMYPMNKDM WDDRMTAMTP DEDVFYAVGL LRSAVAGGSG GDVEQLEREN AAVLELCDLA
     GGGIGCRQYL PHHASRDGWR RHFGAKWGRV ADLKARYDPR AILSPGQGIF PPPPPPSPPP
     PAAGEPITAS