ID   KAO1_ARATH              Reviewed;         490 AA.
AC   O23051; Q9C5Y3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=Ent-kaurenoic acid oxidase 1;
DE            Short=AtKAO1;
DE            EC=1.14.13.79;
DE   AltName: Full=Cytochrome P450 88A3;
GN   Name=KAO1; Synonyms=CYP88A3; OrderedLocusNames=At1g05160;
GN   ORFNames=YUP8H12.23;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Silique;
RX   MEDLINE=21117163; PubMed=11172076; DOI=10.1073/pnas.041588998;
RA   Helliwell C.A., Chandler P.M., Poole A., Dennis E.S., Peacock J.W.;
RT   "The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes
RT   three steps of the gibberellin biosynthesis pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:2065-2070(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=21580400; PubMed=11722763;
RX   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
RT   the plastid and endoplasmic reticulum steps of the gibberellin
RT   biosynthesis pathway.";
RL   Plant J. 28:201-208(2001).
CC   -!- FUNCTION: Catalyzes three successive oxidations of ent-kaurenoic
CC       acid giving gibberellin 12 (GA12), a key step in gibberellins
CC       (GAs) biosynthesis. GAs, which are involved many processes,
CC       including stem elongation, play a central role in plant
CC       development.
CC   -!- CATALYTIC ACTIVITY: Ent-kaur-16-en-19-oate + NADPH + O(2) = ent-7-
CC       alpha-hydroxykaur-16-en-19-oate + NADP(+) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: Ent-7-alpha-hydroxykaur-16-en-19-oate + NADPH
CC       + O(2) = gibberellin A(12) aldehyde + NADP(+) + 2 H(2)O.
CC   -!- CATALYTIC ACTIVITY: Gibberellin A(12) aldehyde + NADPH + O(2) =
CC       gibberellin A(12) + NADP(+) + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in
CC       influorescence stem, influorescence, and silique tissue. Weakly
CC       expressed in cauline and rosette leaves. Expressed at a higher
CC       level in stem and influorescence than AtKAO2/CYP88A4.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AF318500; AAK11564.1; -; mRNA.
DR   EMBL; AC000098; AAB71462.1; -; Genomic_DNA.
DR   IPI; IPI00547281; -.
DR   PIR; H86185; H86185.
DR   RefSeq; NP_172008.1; -.
DR   UniGene; At.10414; -.
DR   HSSP; P14779; 1JPZ.
DR   PRIDE; O23051; -.
DR   GeneID; 839311; -.
DR   GenomeReviews; CT485782_GR; AT1G05160.
DR   KEGG; ath:AT1G05160; -.
DR   GeneFarm; 1616; 94.
DR   TAIR; At1g05160; -.
DR   OMA; O23051; ISNIVER.
DR   BioCyc; MetaCyc:AT1G05160-MON; -.
DR   BRENDA; 1.14.13.79; 302.
DR   ArrayExpress; O23051; -.
DR   GermOnline; AT1G05160; Arabidopsis thaliana.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0051777; F:ent-kaurenoate oxidase activity; IDA:TAIR.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; TAS:TAIR.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Monooxygenase; NADP; Oxidoreductase; Transmembrane.
FT   CHAIN         1    490       Ent-kaurenoic acid oxidase 1.
FT                                /FTId=PRO_0000052178.
FT   TRANSMEM      6     26       Potential.
FT   METAL       439    439       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   490 AA;  56409 MW;  7FD8CD7A8864D298 CRC64;
     MAETTSWIPV WFPLMVLGCF GLNWLVRKVN VWLYESSLGE NRHYLPPGDL GWPFIGNMLS
     FLRAFKTSDP DSFTRTLIKR YGPKGIYKAH MFGNPSIIVT TSDTCRRVLT DDDAFKPGWP
     TSTMELIGRK SFVGISFEEH KRLRRLTAAP VNGHEALSTY IPYIEENVIT VLDKWTKMGE
     FEFLTHLRKL TFRIIMYIFL SSESENVMDA LEREYTALNY GVRAMAVNIP GFAYHRALKA
     RKTLVAAFQS IVTERRNQRK QNILSNKKDM LDNLLNVKDE DGKTLDDEEI IDVLLMYLNA
     GHESSGHTIM WATVFLQEHP EVLQRAKAEQ EMILKSRPEG QKGLSLKETR KMEFLSQVVD
     ETLRVITFSL TAFREAKTDV EMNGYLIPKG WKVLTWFRDV HIDPEVFPDP RKFDPARWDN
     GFVPKAGAFL PFGAGSHLCP GNDLAKLEIS IFLHHFLLKY QVKRSNPECP VMYLPHTRPT
     DNCLARISYQ
//