ID A0A078JD82_BRANA Unreviewed; 518 AA.
AC A0A078JD82;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=cytokinin dehydrogenase {ECO:0000256|ARBA:ARBA00011928};
DE EC=1.5.99.12 {ECO:0000256|ARBA:ARBA00011928};
GN Name=BnaCnng41060D {ECO:0000313|EMBL:CDY62828.1};
GN ORFNames=GSBRNA2T00037652001 {ECO:0000313|EMBL:CDY62828.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY62828.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY62828.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
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 -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; LK034201; CDY62828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078JD82; -.
DR STRING; 3708.A0A078JD82; -.
DR PaxDb; 3708-A0A078JD82; -.
DR EnsemblPlants; CDY62828; CDY62828; GSBRNA2T00037652001.
DR Gramene; CDY62828; CDY62828; GSBRNA2T00037652001.
DR OMA; SSGFDEW; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR ExpressionAtlas; A0A078JD82; baseline and differential.
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; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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 PANTHER; PTHR13878:SF127; CYTOKININ DEHYDROGENASE 3; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR Pfam; PF09265; Cytokin-bind; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..518
FT /note="cytokinin dehydrogenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001739249"
FT DOMAIN 66..243
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 518 AA; 58856 MW; 7388FDBAF503455E CRC64;
MASNNFPSQS HLLVIIIFIT TLLTPITTNN TSPQPWNILS NDNFAGKLTS ASSSVEAAAI
DFGHVTKILP SAVLNPSSVQ DIIDLIKLSF DSQSSFPIAA RGHGHSFRGQ AAAKDGVVVN
MRSMVNEDRG IKVSRTGLYA DVDTAWLWIE VLNKTLELGL TPVSWTDYLY LTIGGTLSNG
GISGQTSRYG PQISNVLELD VITGKGEIAT CSNDTNSDLF YAALGGLGQF GIITRARIKL
ELAPKRAKWL RFLYTDFSEF TRDQERLISE TDGLHFLEGS VMLDHGPPDN WRSTYYPPSD
HLRIVSMIKR YRVIYCLEVA KYYDETSQHS VNEEIEKLSE SLNYVRGFVY EKDVTYIDFL
NRVRTGELNL KSKGQWDVPH PWLNLFVPKS QISRFDYGVF KGIILRNNIT TGPLLVYPMK
RIMWNDQMST AIPEEDVFYA VGFLRSAEFD NWEAYDKENM EVLKFCEDAK MDVIQYLPYH
ASQEGWVRHF GPMWNTFVER KYRYDPKMIL SPGQNIFR
//
