KO_SALMI
ID KO_SALMI Reviewed; 519 AA.
AC A0A0G2RKY1; A0A0B4VT08;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Ent-kaurene oxidase {ECO:0000303|PubMed:26971881};
DE Short=SmKO {ECO:0000303|PubMed:26971881};
DE EC=1.14.14.86 {ECO:0000269|PubMed:26971881};
DE AltName: Full=Cytochrome P450 701A40 {ECO:0000303|PubMed:25493946};
GN Name=KO {ECO:0000303|PubMed:26971881};
GN Synonyms=CYP701A40 {ECO:0000303|PubMed:25493946};
OS Salvia miltiorrhiza (Chinese sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=226208;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=25493946; DOI=10.1371/journal.pone.0115149;
RA Chen H., Wu B., Nelson D.R., Wu K., Liu C.;
RT "Computational identification and systematic classification of novel
RT Cytochrome P450 genes in Salvia miltiorrhiza.";
RL PLoS ONE 9:E115149-E115149(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26971881; DOI=10.1038/srep23057;
RA Su P., Tong Y., Cheng Q., Hu Y., Zhang M., Yang J., Teng Z., Gao W.,
RA Huang L.;
RT "Functional characterization of ent-copalyl diphosphate synthase, kaurene
RT synthase and kaurene oxidase in the Salvia miltiorrhiza gibberellin
RT biosynthetic pathway.";
RL Sci. Rep. 6:23057-23057(2016).
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 (PubMed:26971881). GAs, which are involved many processes,
CC including stem elongation, play a central role in plant development
CC (Probable). {ECO:0000269|PubMed:26971881, ECO:0000305|PubMed:26971881}.
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:26971881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32324;
CC Evidence={ECO:0000269|PubMed:26971881};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000250|UniProtKB:Q93ZB2}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KP337739; AJD25233.1; -; mRNA.
DR EMBL; KJ606394; AJF93403.1; -; mRNA.
DR AlphaFoldDB; A0A0G2RKY1; -.
DR SMR; A0A0G2RKY1; -.
DR BRENDA; 1.14.14.86; 9850.
DR UniPathway; UPA00390; -.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:UniProt.
DR GO; GO:0010241; P:ent-kaurene oxidation to kaurenoic acid; IEA:InterPro.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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;
KW Oxidoreductase; Plastid; Plastid outer membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..519
FT /note="Ent-kaurene oxidase"
FT /id="PRO_0000449937"
FT TOPO_DOM 1..10
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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|UniProtKB:Q96242"
FT CONFLICT 106
FT /note="I -> V (in Ref. 1; AJD25233)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="R -> Q (in Ref. 1; AJD25233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 58880 MW; 1BCF20DF0FA01758 CRC64;
MDTLLSLQAV PAAAAIGGPV VAIGGITLFF IREYVKDQRK KSSSFPPPPK VPGLPVIGNL
LQLKEKKPHK TFTKWSEKYG PIYSIRTGAN TMIVLNTNDV AKEAMITKYS SISTRKLSKA
LTILTSDKSI VAMSDYNEFY KAAKRHLLTS TLGPTAQKRH RVHRNLMINN ICDQFLAHAK
MYPSEAVNFR KIFQSELFGL SMKQAIGEDV ESIYVEDLDT TLSRQEMFKI LVVDPMEGAI
DVDWRDFFPY LKWIPNQHFE NKIQQMHFHR EAVMKALIEQ QKKRIASGKA INCYLDHLLS
EAADTLSEQQ ILMLLWEAII EASDTTLVTT EWAMYELSKD PKRQNYLLSE IQNACGFDQL
NEEKLCRLPY LAAIFQETLR KHSPVPVVPL RYVHEETQLG GYTIPEGSEI AINIYGCNMD
KNVWDSPEEW RPERFVFGKD DTTELHKTMA FGGGKRVCAG ALQAMTISCI AIGRLVQELE
WRLGDGEEAN VDTLGLTTHK LHPLQTIIKP RLRDRVCVS
