KAO1_ARATH
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 03-AUG-2022, entry version 165.
DE RecName: Full=Ent-kaurenoic acid oxidase 1;
DE Short=AtKAO1;
DE EC=1.14.14.107 {ECO:0000269|PubMed:11172076};
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Silique;
RX PubMed=11172076; DOI=10.1073/pnas.98.4.2065;
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 three
RT 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 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 [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 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).
CC -!- FUNCTION: Catalyzes three successive oxidations of ent-kaurenoic acid
CC giving gibberellin 12 (GA12), 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:11172076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-kaur-16-en-19-oate + 3 O2 + 3 reduced [NADPH--hemoprotein
CC reductase] = gibberellin A12 + 4 H(+) + 4 H2O + 3 oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:33219, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57297, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58627; EC=1.14.14.107;
CC Evidence={ECO:0000269|PubMed:11172076};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum 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 stem, influorescence, and silique tissue. Weakly
CC expressed in cauline and rosette leaves. Expressed at a higher level in
CC stem and influorescence than AtKAO2/CYP88A4.
CC {ECO:0000269|PubMed:11172076}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF318500; AAK11564.1; -; mRNA.
DR EMBL; AC000098; AAB71462.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27796.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57713.1; -; Genomic_DNA.
DR PIR; H86185; H86185.
DR RefSeq; NP_001320198.1; NM_001331521.1.
DR RefSeq; NP_172008.1; NM_100394.4.
DR AlphaFoldDB; O23051; -.
DR SMR; O23051; -.
DR BioGRID; 24546; 1.
DR STRING; 3702.AT1G05160.1; -.
DR PaxDb; O23051; -.
DR PRIDE; O23051; -.
DR ProteomicsDB; 250629; -.
DR EnsemblPlants; AT1G05160.1; AT1G05160.1; AT1G05160.
DR EnsemblPlants; AT1G05160.2; AT1G05160.2; AT1G05160.
DR GeneID; 839311; -.
DR Gramene; AT1G05160.1; AT1G05160.1; AT1G05160.
DR Gramene; AT1G05160.2; AT1G05160.2; AT1G05160.
DR KEGG; ath:AT1G05160; -.
DR Araport; AT1G05160; -.
DR TAIR; locus:2207240; AT1G05160.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; O23051; -.
DR OMA; EMGWPMV; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; O23051; -.
DR BioCyc; ARA:AT1G05160-MON; -.
DR BioCyc; MetaCyc:AT1G05160-MON; -.
DR BRENDA; 1.14.13.79; 399.
DR BRENDA; 1.14.14.107; 399.
DR UniPathway; UPA00390; -.
DR PRO; PR:O23051; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O23051; baseline and differential.
DR Genevisible; O23051; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051777; F:ent-kaurenoate oxidase activity; IDA: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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR GO; GO:0009686; P:gibberellin biosynthetic process; TAS:TAIR.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..490
FT /note="Ent-kaurenoic acid oxidase 1"
FT /id="PRO_0000052178"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 439
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 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
