KO1_ARATH
ID KO1_ARATH Reviewed; 509 AA.
AC Q93ZB2; O81188; Q9S7C8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ent-kaurene oxidase, chloroplastic;
DE Short=AtKO1;
DE EC=1.14.14.86 {ECO:0000269|PubMed:20698828, ECO:0000269|PubMed:9952446};
DE AltName: Full=Cytochrome P450 701A3;
GN Name=KO; Synonyms=CYP701A3, GA3, KO1; OrderedLocusNames=At5g25900;
GN ORFNames=T1N24.23;
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 [GENOMIC DNA / MRNA], FUNCTION, ENZYME ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Silique;
RX PubMed=9671797; DOI=10.1073/pnas.95.15.9019;
RA Helliwell C.A., Sheldon C.C., Olive M.R., Walker A.R., Zeevaart J.A.D.,
RA Peacock W.J., Dennis E.S.;
RT "Cloning of the Arabidopsis ent-kaurene oxidase gene GA3.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9019-9024(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP CATALYTIC ACTIVITY.
RX PubMed=9952446; DOI=10.1104/pp.119.2.507;
RA Helliwell C.A., Poole A., Peacock W.J., Dennis E.S.;
RT "Arabidopsis ent-kaurene oxidase catalyzes three steps of gibberellin
RT biosynthesis.";
RL Plant Physiol. 119:507-510(1999).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11722763; DOI=10.1046/j.1365-313x.2001.01150.x;
RA Helliwell C.A., Sullivan J.A., Mould R.M., Gray J.C., Peacock W.J.,
RA Dennis E.S.;
RT "A plastid envelope location of Arabidopsis ent-kaurene oxidase links the
RT plastid and endoplasmic reticulum steps of the gibberellin biosynthesis
RT pathway.";
RL Plant J. 28:201-208(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11737781; DOI=10.1046/j.1365-313x.2001.01168.x;
RA Yamaguchi S., Kamiya Y., Sun T.-P.;
RT "Distinct cell-specific expression patterns of early and late gibberellin
RT biosynthetic genes during Arabidopsis seed germination.";
RL Plant J. 28:443-453(2001).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20698828; DOI=10.1042/bj20100597;
RA Morrone D., Chen X., Coates R.M., Peters R.J.;
RT "Characterization of the kaurene oxidase CYP701A3, a multifunctional
RT cytochrome P450 from gibberellin biosynthesis.";
RL Biochem. J. 431:337-344(2010).
CC -!- FUNCTION: Catalyzes three successive oxidations of the 4-methyl group
CC of ent-kaurene giving kaurenoic acid, a key step in gibberellins (GAs)
CC biosynthesis. GAs, which are involved many processes, including stem
CC elongation, play a central role in plant development.
CC {ECO:0000269|PubMed:20698828, ECO:0000269|PubMed:9671797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-kaur-16-ene + 3 O2 + 3 reduced [NADPH--hemoprotein
CC reductase] = ent-kaur-16-en-19-oate + 4 H(+) + 4 H2O + 3 oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:32323, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15415,
CC ChEBI:CHEBI:57297, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC EC=1.14.14.86; Evidence={ECO:0000269|PubMed:20698828,
CC ECO:0000269|PubMed:9952446};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for ent-kaurene {ECO:0000269|PubMed:20698828};
CC KM=6 uM for ent-kaurenol {ECO:0000269|PubMed:20698828};
CC KM=1.9 uM for ent-kaurenal {ECO:0000269|PubMed:20698828};
CC KM=10 uM for ent-isokaurene {ECO:0000269|PubMed:20698828};
CC KM=28 uM for ent-beyerene {ECO:0000269|PubMed:20698828};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:11722763}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11722763}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in
CC influorescence tissues. In germinating seeds, it is mainly localized in
CC the cortex and endodermis of embryo axis. {ECO:0000269|PubMed:11737781,
CC ECO:0000269|PubMed:9671797}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL15302.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF047719; AAC39505.1; -; mRNA.
DR EMBL; AF047720; AAC39506.1; -; Genomic_DNA.
DR EMBL; AF047721; AAC39507.1; -; Genomic_DNA.
DR EMBL; AF149413; AAD40137.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93499.1; -; Genomic_DNA.
DR EMBL; AY057671; AAL15302.1; ALT_FRAME; mRNA.
DR PIR; T51806; T51806.
DR RefSeq; NP_197962.1; NM_122491.3.
DR AlphaFoldDB; Q93ZB2; -.
DR SMR; Q93ZB2; -.
DR BioGRID; 17934; 1.
DR STRING; 3702.AT5G25900.1; -.
DR SwissPalm; Q93ZB2; -.
DR PaxDb; Q93ZB2; -.
DR PRIDE; Q93ZB2; -.
DR ProteomicsDB; 250696; -.
DR EnsemblPlants; AT5G25900.1; AT5G25900.1; AT5G25900.
DR GeneID; 832659; -.
DR Gramene; AT5G25900.1; AT5G25900.1; AT5G25900.
DR KEGG; ath:AT5G25900; -.
DR Araport; AT5G25900; -.
DR TAIR; locus:2180572; AT5G25900.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q93ZB2; -.
DR OMA; STFMQWI; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q93ZB2; -.
DR BioCyc; MetaCyc:AT5G25900-MON; -.
DR BRENDA; 1.14.14.86; 399.
DR SABIO-RK; Q93ZB2; -.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q93ZB2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93ZB2; baseline and differential.
DR Genevisible; Q93ZB2; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052617; F:ent-kaur-16-en-19-al oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052616; F:ent-kaur-16-en-19-ol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052615; F:ent-kaurene oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0010241; P:ent-kaurene oxidation to kaurenoic acid; IMP:TAIR.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IDA:TAIR.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR044225; KO_chloroplastic.
DR PANTHER; PTHR47283; PTHR47283; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP;
KW Oxidoreductase; Plastid; Plastid outer membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Ent-kaurene oxidase, chloroplastic"
FT /id="PRO_0000052181"
FT TOPO_DOM 1..2
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 454
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"
FT CONFLICT 97
FT /note="A -> G (in Ref. 1; AAC39507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 58160 MW; A84F7E2C78F0E83F CRC64;
MAFFSMISIL LGFVISSFIF IFFFKKLLSF SRKNMSEVST LPSVPVVPGF PVIGNLLQLK
EKKPHKTFTR WSEIYGPIYS IKMGSSSLIV LNSTETAKEA MVTRFSSIST RKLSNALTVL
TCDKSMVATS DYDDFHKLVK RCLLNGLLGA NAQKRKRHYR DALIENVSSK LHAHARDHPQ
EPVNFRAIFE HELFGVALKQ AFGKDVESIY VKELGVTLSK DEIFKVLVHD MMEGAIDVDW
RDFFPYLKWI PNKSFEARIQ QKHKRRLAVM NALIQDRLKQ NGSESDDDCY LNFLMSEAKT
LTKEQIAILV WETIIETADT TLVTTEWAIY ELAKHPSVQD RLCKEIQNVC GGEKFKEEQL
SQVPYLNGVF HETLRKYSPA PLVPIRYAHE DTQIGGYHVP AGSEIAINIY GCNMDKKRWE
RPEDWWPERF LDDGKYETSD LHKTMAFGAG KRVCAGALQA SLMAGIAIGR LVQEFEWKLR
DGEEENVDTY GLTSQKLYPL MAIINPRRS
