CKX8_ORYSI
ID CKX8_ORYSI Reviewed; 532 AA.
AC A2XVN3; Q7XKG1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Cytokinin dehydrogenase 8;
DE EC=1.5.99.12;
DE AltName: Full=Cytokinin oxidase 8;
DE Short=OsCKX8;
DE Flags: Precursor;
GN Name=CKX8; ORFNames=OsI_16693, OSIGBa0153E02-OSIGBa0093I20.7;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(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; CR855229; CAH67878.1; -; Genomic_DNA.
DR EMBL; CM000129; EAY94893.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XVN3; -.
DR SMR; A2XVN3; -.
DR STRING; 39946.A2XVN3; -.
DR EnsemblPlants; BGIOSGA016782-TA; BGIOSGA016782-PA; BGIOSGA016782.
DR Gramene; BGIOSGA016782-TA; BGIOSGA016782-PA; BGIOSGA016782.
DR HOGENOM; CLU_024955_1_0_1; -.
DR OMA; DGSRADH; -.
DR Proteomes; UP000007015; Chromosome 4.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..532
FT /note="Cytokinin dehydrogenase 8"
FT /id="PRO_0000394212"
FT DOMAIN 51..238
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 87..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 92..93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 162
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 173..177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 517..520
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 92
FT /note="Pros-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 57619 MW; 78D3740726B60A2C CRC64;
MELKAMYLYA AVLAVLLCSS VNFIQSPTDV LGPVALLEPT PSSARDFGAV VSDAPFAVMR
PESPDDIALL LGALSSTAPS PRATVAAVGA GHSLHGQAQA RDGIVVETRA LPRDVHVVSA
RAHGGDDDAT VRAYADVGAG ALWVEVLEEC LKLGLAPPSW TDYLYLTVGG TLSNGGISGQ
TFKHGPQISN VLQLEVVTGK GEVVTCSPTE IPELFFAVLG GLGQFGIITR ARIPLQLAPP
KVRWVRAFYD SFETFTGDQE LLVSMPEQVD YVEGFMVLNE QSLHSSSVAF PAQLNFSPDF
GSKGRKKVYY CIEFAVHDFQ QDSSRADHVV KLVSAKLSYL RPHVYSVEVS YFDFLNRVRM
EEESLRSRGL WDVPHPWLNV FVPKHGITQF KGLLMDTVSA DDFEGPILVY PLLTDKWDGN
TSAVVPAAPD GVMYIFGVLR STDPARCGRA CVDSIMARHR RVADEACRDG GGGGRGIGAK
QYLARQPSPA RWRDHFGAGW GRFAARKARF DPLHVLGPGQ GIFPRTDSAG SM
