C7351_ARATH
ID C7351_ARATH Reviewed; 518 AA.
AC Q9FF18;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cytokinin hydroxylase;
DE EC=1.14.13.-;
DE AltName: Full=Cytochrome P450 35A1;
GN Name=CYP735A1; OrderedLocusNames=At5g38450; ORFNames=MXI10.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15280363; DOI=10.1074/jbc.m406337200;
RA Takei K., Yamaya T., Sakakibara H.;
RT "Arabidopsis CYP735A1 and CYP735A2 encode cytokinin hydroxylases that
RT catalyze the biosynthesis of trans-Zeatin.";
RL J. Biol. Chem. 279:41866-41872(2004).
CC -!- FUNCTION: Cytokinin hydroxylase that catalyzes the biosynthesis of
CC trans-zeatin via the isopentenyladenine riboside 5'-monophosphate
CC (iPRMP)-dependent pathway. Can use isopentenyladenosine-5'-
CC monophosphate, isopentenyladenosine-5'-diphosphate and
CC isopentenyladenosine-5'-triphosphate as substrate.
CC {ECO:0000269|PubMed:15280363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-(dimethylallyl)adenosine 5'-phosphate + NADPH + O2
CC = 9-ribosyl-trans-zeatin 5'-phosphate + H2O + NADP(+);
CC Xref=Rhea:RHEA:47812, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87947;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-(dimethylallyl)adenosine 5'-diphosphate + NADPH +
CC O2 = 9-ribosyl-trans-zeatin 5'-diphosphate + H2O + NADP(+);
CC Xref=Rhea:RHEA:47816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:73533, ChEBI:CHEBI:87950;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-(dimethylallyl)adenosine 5'-triphosphate + NADPH +
CC O2 = 9-ribosyl-trans-zeatin 5'-triphosphate + H2O + NADP(+);
CC Xref=Rhea:RHEA:47820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:73532, ChEBI:CHEBI:87953;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.76 uM for isopentenyladenine riboside 5'-monophosphate
CC {ECO:0000269|PubMed:15280363};
CC KM=2.28 uM for isopentenyladenine riboside 5'-diphosphate
CC {ECO:0000269|PubMed:15280363};
CC KM=8.32 uM for isopentenyladenine riboside 5'-triphosphate
CC {ECO:0000269|PubMed:15280363};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:15280363}.
CC -!- INDUCTION: By trans-zeatin and isopentenyladenine in roots. Down-
CC regulated by auxin and abscisic acid in roots.
CC {ECO:0000269|PubMed:15280363}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX832759; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB005248; BAB09357.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94318.1; -; Genomic_DNA.
DR EMBL; BX832759; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_198661.1; NM_123206.3.
DR AlphaFoldDB; Q9FF18; -.
DR SMR; Q9FF18; -.
DR STRING; 3702.AT5G38450.1; -.
DR PaxDb; Q9FF18; -.
DR PRIDE; Q9FF18; -.
DR EnsemblPlants; AT5G38450.1; AT5G38450.1; AT5G38450.
DR GeneID; 833833; -.
DR Gramene; AT5G38450.1; AT5G38450.1; AT5G38450.
DR KEGG; ath:AT5G38450; -.
DR Araport; AT5G38450; -.
DR TAIR; locus:2177411; AT5G38450.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_0_1; -.
DR InParanoid; Q9FF18; -.
DR OMA; LFGHAQE; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q9FF18; -.
DR SABIO-RK; Q9FF18; -.
DR PRO; PR:Q9FF18; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF18; baseline and differential.
DR Genevisible; Q9FF18; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0033466; P:trans-zeatin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..518
FT /note="Cytokinin hydroxylase"
FT /id="PRO_0000411208"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 464
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 518 AA; 58900 MW; C1B0AC901BE4FA32 CRC64;
MLLTILKSLL VIFVTTILRV LYDTISCYWL TPRRIKKIME QQGVTGPKPR PLTGNILEIS
AMVSQSASKD CDSIHHDIVG RLLPHYVAWS KQYGKRFIVW NGTDPRLCLT ETELIKELLM
KHNGVSGRSW LQQQGTKNFI GRGLLMANGQ DWHHQRHLAA PAFTGERLKG YARHMVECTS
KLVERLRKEV GEGANEVEIG EEMHKLTADI ISRTKFGSSF EKGKELFNHL TVLQRRCAQA
TRHLCFPGSR FLPSKYNREI KSLKKEVERL LIEIIQSRRD CAEMGRSSTH GDDLLGLLLN
EMDIDKNNNN NNNNLQLIMD ECKTFFFAGH ETTALLLTWT TMLLADNPTW QEKVREEVRE
VFGRNGLPSV DQLSKLTSLS KVINESLRLY PPATLLPRMA FEDLKLGDLT IPKGLSIWIP
VLAIHHSEEL WGKDANQFNP ERFGGRPFAS GRHFIPFAAG PRNCIGQQFA LMEAKIILAT
LISKFNFTIS KNYRHAPIVV LTIKPKYGVQ VILKPLVS
