C7352_ARATH
ID C7352_ARATH Reviewed; 512 AA.
AC Q9ZW95;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cytokinin hydroxylase;
DE EC=1.14.13.-;
DE AltName: Full=Cytochrome P450 35A2;
GN Name=CYP735A2; OrderedLocusNames=At1g67110; ORFNames=F5A8.3;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, 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=0.39 uM for isopentenyladenine riboside 5'-monophosphate;
CC KM=0.76 uM for isopentenyladenine riboside 5'-diphosphate;
CC KM=4.9 uM for isopentenyladenine riboside 5'-triphosphate;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC {ECO:0000269|PubMed:15280363}.
CC -!- INDUCTION: By trans-zeatin, cis-zeatin and isopentenyladenine in roots.
CC Down-regulated by auxin and abscisic acid in roots.
CC {ECO:0000269|PubMed:15280363}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004146; AAD10659.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34597.1; -; Genomic_DNA.
DR EMBL; BT011622; AAS47628.1; -; mRNA.
DR EMBL; BT012626; AAT06445.1; -; mRNA.
DR PIR; A96695; A96695.
DR RefSeq; NP_176882.1; NM_105381.5.
DR AlphaFoldDB; Q9ZW95; -.
DR SMR; Q9ZW95; -.
DR STRING; 3702.AT1G67110.1; -.
DR PaxDb; Q9ZW95; -.
DR PRIDE; Q9ZW95; -.
DR EnsemblPlants; AT1G67110.1; AT1G67110.1; AT1G67110.
DR GeneID; 843031; -.
DR Gramene; AT1G67110.1; AT1G67110.1; AT1G67110.
DR KEGG; ath:AT1G67110; -.
DR Araport; AT1G67110; -.
DR TAIR; locus:2033656; AT1G67110.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_0_1; -.
DR InParanoid; Q9ZW95; -.
DR OMA; ELYPMMW; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q9ZW95; -.
DR SABIO-RK; Q9ZW95; -.
DR PRO; PR:Q9ZW95; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZW95; baseline and differential.
DR Genevisible; Q9ZW95; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; 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..512
FT /note="Cytokinin hydroxylase"
FT /id="PRO_0000411209"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 458
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 512 AA; 58463 MW; 038844E878935BC7 CRC64;
MMVTLVLKYV LVIVMTLILR VLYDSICCYF LTPRRIKKFM ERQGITGPKP RLLTGNIIDI
SKMLSHSASN DCSSIHHNIV PRLLPHYVSW SKQYGKRFIM WNGTEPRLCL TETEMIKELL
TKHNPVTGKS WLQQQGTKGF IGRGLLMANG EAWHHQRHMA APAFTRDRLK GYAKHMVECT
KMMAERLRKE VGEEVEIGEE MRRLTADIIS RTEFGSSCDK GKELFSLLTV LQRLCAQATR
HLCFPGSRFL PSKYNREIKS LKTEVERLLM EIIDSRKDSV EIGRSSSYGD DLLGLLLNQM
DSNKNNLNVQ MIMDECKTFF FTGHETTSLL LTWTLMLLAH NPTWQDNVRD EVRQVCGQDG
VPSVEQLSSL TSLNKVINES LRLYPPATLL PRMAFEDIKL GDLIIPKGLS IWIPVLAIHH
SNELWGEDAN EFNPERFTTR SFASSRHFMP FAAGPRNCIG QTFAMMEAKI ILAMLVSKFS
FAISENYRHA PIVVLTIKPK YGVQLVLKPL DL
