ID B9RK75_RICCO Unreviewed; 529 AA.
AC B9RK75;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=cytokinin dehydrogenase {ECO:0000256|ARBA:ARBA00011928};
DE EC=1.5.99.12 {ECO:0000256|ARBA:ARBA00011928};
GN ORFNames=RCOM_1047010 {ECO:0000313|EMBL:EEF48073.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ973784; EEF48073.1; -; Genomic_DNA.
DR AlphaFoldDB; B9RK75; -.
DR STRING; 3988.B9RK75; -.
DR eggNOG; KOG1231; Eukaryota.
DR InParanoid; B9RK75; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EEF48073.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT DOMAIN 65..249
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 529 AA; 59640 MW; 5C303B56A6F21A98 CRC64;
MAENYAFPAY FIVILFITRL VSTVGKVKPL TTLLPPKLLT LDFAERIHTD PSSIKSASSD
YGNLVHKKPA AVLYPSSVQD IVSLINFAYN YSAPLTVSAR GRSHSINGQA MAPDGVVVDM
MHLRSIIEKT NGGVTVSKDP LLGFYADVGG EQLWIDVLNA TIEHGLAPVS WTDYLYLTVG
GTLSNAGISG QSFRYGPQIS NVYEMDVVTG RGELVTCSGH RNSDLFYAVL GGLGQFGIIT
RARIALEPAP KKVKWVRMLY SDFSEFTKDQ ERLISINGRK QSNALDYVEG SLLMNQGPPN
NWRSSFFPSS DIPRIMSLVT QHGIIYCLEV AKYYDDATQH SMSMELQLMF KGLSFADGFM
FEKDVPYVDF LDRVRSGEIK LQSQGLWDVP HPWLNLFLPK SSISDFNSGV FRDIVLKRNV
TTGPVLVYPM NRNKWDDRTS AVIPDEDVFY TVGFLHSSGF DDWQTYDDQN KDLLNYCDKA
GIKVKQYFPH YTTKEEWTDH FGSKWRTFVE RKAKFDPKRM LSPGQRIFN
//
