KAO2_ARATH
ID KAO2_ARATH Reviewed; 489 AA.
AC Q9C5Y2; Q9ZV72;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ent-kaurenoic acid oxidase 2;
DE Short=AtKAO2;
DE EC=1.14.14.107 {ECO:0000269|PubMed:11172076};
DE AltName: Full=Cytochrome P450 88A4;
GN Name=KAO2; Synonyms=CYP88A4; OrderedLocusNames=At2g32440; ORFNames=T32F6.4;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 weaker level in
CC stem and influorescence than AtKAO1/CYP88A3.
CC {ECO:0000269|PubMed:11172076}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF318501; AAK11565.1; -; mRNA.
DR EMBL; AC005700; AAC69934.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08685.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08686.1; -; Genomic_DNA.
DR PIR; B84733; B84733.
DR RefSeq; NP_001189657.1; NM_001202728.1.
DR RefSeq; NP_180803.1; NM_128803.4.
DR AlphaFoldDB; Q9C5Y2; -.
DR SMR; Q9C5Y2; -.
DR STRING; 3702.AT2G32440.2; -.
DR PaxDb; Q9C5Y2; -.
DR PRIDE; Q9C5Y2; -.
DR ProteomicsDB; 250612; -.
DR EnsemblPlants; AT2G32440.1; AT2G32440.1; AT2G32440.
DR EnsemblPlants; AT2G32440.2; AT2G32440.2; AT2G32440.
DR GeneID; 817805; -.
DR Gramene; AT2G32440.1; AT2G32440.1; AT2G32440.
DR Gramene; AT2G32440.2; AT2G32440.2; AT2G32440.
DR KEGG; ath:AT2G32440; -.
DR Araport; AT2G32440; -.
DR TAIR; locus:2062623; AT2G32440.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q9C5Y2; -.
DR OMA; CPVMFLP; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q9C5Y2; -.
DR BioCyc; ARA:AT2G32440-MON; -.
DR BioCyc; MetaCyc:AT2G32440-MON; -.
DR BRENDA; 1.14.13.79; 399.
DR BRENDA; 1.14.14.107; 399.
DR UniPathway; UPA00390; -.
DR PRO; PR:Q9C5Y2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9C5Y2; baseline and differential.
DR Genevisible; Q9C5Y2; 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..489
FT /note="Ent-kaurenoic acid oxidase 2"
FT /id="PRO_0000052179"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 436
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 288
FT /note="E -> K (in Ref. 1; AAK11565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 56750 MW; 945F204F6CB251DA CRC64;
MTETGLILMW FPLIILGLFV LKWVLKRVNV WIYVSKLGEK KHYLPPGDLG WPVIGNMWSF
LRAFKTSDPE SFIQSYITRY GRTGIYKAHM FGYPCVLVTT PETCRRVLTD DDAFHIGWPK
STMKLIGRKS FVGISFEEHK RLRRLTSAPV NGPEALSVYI QFIEETVNTD LEKWSKMGEI
EFLSHLRKLT FKVIMYIFLS SESEHVMDSL EREYTNLNYG VRAMGINLPG FAYHRALKAR
KKLVAAFQSI VTNRRNQRKQ NISSNRKDML DNLIDVKDEN GRVLDDEEII DLLLMYLNAG
HESSGHLTMW ATILMQEHPM ILQKAKEEQE RIVKKRAPGQ KLTLKETREM VYLSQVIDET
LRVITFSLTA FREAKSDVQM DGYIIPKGWK VLTWFRNVHL DPEIYPDPKK FDPSRWEGYT
PKAGTFLPFG LGSHLCPGND LAKLEISIFL HHFLLKYRVE RSNPGCPVMF LPHNRPKDNC
LARITRTMP
