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Database: UniProt
Entry: M0ZHH7_SOLTU
LinkDB: M0ZHH7_SOLTU
Original site: M0ZHH7_SOLTU 
ID   M0ZHH7_SOLTU            Unreviewed;       699 AA.
AC   M0ZHH7;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=cytokinin dehydrogenase {ECO:0000256|ARBA:ARBA00011928};
DE            EC=1.5.99.12 {ECO:0000256|ARBA:ARBA00011928};
GN   Name=102591248 {ECO:0000313|EnsemblPlants:PGSC0003DMT400000883};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400000883, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400000883}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400000883};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00001689};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000256|ARBA:ARBA00004913}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   AlphaFoldDB; M0ZHH7; -.
DR   SMR; M0ZHH7; -.
DR   STRING; 4113.M0ZHH7; -.
DR   PaxDb; 4113-PGSC0003DMT400000883; -.
DR   EnsemblPlants; PGSC0003DMT400000883; PGSC0003DMT400000883; PGSC0003DMG400000335.
DR   Gramene; PGSC0003DMT400000883; PGSC0003DMT400000883; PGSC0003DMG400000335.
DR   eggNOG; KOG1231; Eukaryota.
DR   HOGENOM; CLU_394535_0_0_1; -.
DR   InParanoid; M0ZHH7; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009690; P:cytokinin metabolic process; IEA:InterPro.
DR   CDD; cd11393; bHLH_AtbHLH_like; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR045239; bHLH95_bHLH.
DR   InterPro; IPR011598; bHLH_dom.
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; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   PANTHER; PTHR13878:SF172; CYTOKININ DEHYDROGENASE; 1.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF09265; Cytokin-bind; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism {ECO:0000256|ARBA:ARBA00022589};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          46..229
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          532..581
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
SQ   SEQUENCE   699 AA;  79315 MW;  FEB0B59243154AB1 CRC64;
     MSNLGKLKSW NPSIPQEIFS LNISSKLSTN SDDIKESSKD FGKIVQKKFP AAVLYPSCVN
     DIIDLIQFSY DLSVPFQVAA KGHGHSIRGQ AMAQNGVIVE MNSLNNNNNE NCGVRVSWDL
     DLGFYADVGG EQLWIDVLRS TLEYGLAPVS WTDYLYLTVG GTLSNAGISG QTFRYGPQIS
     NVHEMDVITG KGELVTCSKD KNSELFFGVL GGLGQFGIII RAKIVLDKAP TRVKWVRMLY
     DDFPKFTKDQ EYLISIHHNG LDYVEGSLMM EQSSLNNWRS SFFSPSNQAK IVSLLSQNKI
     MYCLEMVKYY DDHTANTIDE ELKKLVQGLN YLGGFMFKKD VTFVEFLNRV RKGQIELELK
     GMWDVPHPWL NLFVPKSNIM QFNAAVFEDI ILRQNKPTGP ILVYPTSRKS EYSSLFHNVA
     KTCYVTQENQ TLTQFPKIEG EDDVIRQAYL AVISSSSPSS SSRGQIQEIL TRDHRLVTRN
     TTAFTRFRST NYASIGATSS CRQNMLKRSI TFFKNLYTMN RQEGIQVNRA MSTQVHHMIS
     ERRRREKLNE NFQHLRSLLP PEIKKDKASV LASTTEYLSS LKDQVEKLCK RNEILEATLL
     SKKEVSQFQQ NGSGRVYIYI TNIEERIVDL QVIAKGKCNT LDLVICLMEF LKMASYVNLM
     AIDANTTMVQ SCPLTQITLR LRIQVIYVSH SVFDICIGD
//
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