C7D55_HYOMU
ID C7D55_HYOMU Reviewed; 502 AA.
AC A6YIH8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Premnaspirodiene oxygenase;
DE Short=HPO;
DE EC=1.14.14.151 {ECO:0000269|PubMed:17715131};
DE AltName: Full=Cytochrome P450 71D55;
GN Name=CYP71D55;
OS Hyoscyamus muticus (Egyptian henbane).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC Hyoscyamus.
OX NCBI_TaxID=35626;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF VAL-366; VAL-480; VAL-482 AND ALA-484.
RX PubMed=17715131; DOI=10.1074/jbc.m703378200;
RA Takahashi S., Yeo Y.S., Zhao Y., O'Maille P.E., Greenhagen B.T., Noel J.P.,
RA Coates R.M., Chappell J.;
RT "Functional characterization of premnaspirodiene oxygenase, a cytochrome
RT P450 catalyzing regio- and stereo-specific hydroxylations of diverse
RT sesquiterpene substrates.";
RL J. Biol. Chem. 282:31744-31754(2007).
CC -!- FUNCTION: Involved in the biosynthesis of solavetivone, a potent
CC antifungal phytoalexin. Catalyzes the successive and independent
CC hydroxylations of premnaspirodiene and solavetivol. The first
CC hydroxylation step is 3-fold more efficient than the second
CC hydroxylation reaction.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-vetispiradiene + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC reductase] + solavetivone; Xref=Rhea:RHEA:32455, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:9192,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:46971, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC EC=1.14.14.151; Evidence={ECO:0000269|PubMed:17715131};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.0 uM for premnaspirodiene {ECO:0000269|PubMed:17715131};
CC KM=1.2 uM for solavetivol {ECO:0000269|PubMed:17715131};
CC KM=11.5 uM for valencene {ECO:0000269|PubMed:17715131};
CC KM=3.3 uM for 5-epi-aristolochene {ECO:0000269|PubMed:17715131};
CC KM=7.8 uM for epi-eremophilene {ECO:0000269|PubMed:17715131};
CC KM=26.5 uM for cedr-8-ene {ECO:0000269|PubMed:17715131};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF569601; ABS00393.1; -; mRNA.
DR AlphaFoldDB; A6YIH8; -.
DR SMR; A6YIH8; -.
DR PRIDE; A6YIH8; -.
DR KEGG; ag:ABS00393; -.
DR BioCyc; MetaCyc:MON-16034; -.
DR BRENDA; 1.14.13.121; 2739.
DR BRENDA; 1.14.14.151; 2739.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..502
FT /note="Premnaspirodiene oxygenase"
FT /id="PRO_0000409471"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 440
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 MUTAGEN 366
FT /note="V->S: Decreases catalytic activity. Strongly
FT increased catalytic activity; when associated with I-482
FT and I-484."
FT /evidence="ECO:0000269|PubMed:17715131"
FT MUTAGEN 480
FT /note="V->S: Increases catalytic activity. Strongly
FT increased catalytic activity; when associated with I-484 or
FT I-482 and I-484."
FT /evidence="ECO:0000269|PubMed:17715131"
FT MUTAGEN 482
FT /note="V->I: Increases catalytic activity. Strongly
FT increased catalytic activity; when associated with I-484 or
FT S-366 and I-484 or S-480 and I-484."
FT /evidence="ECO:0000269|PubMed:17715131"
FT MUTAGEN 484
FT /note="A->I: Decreases catalytic activity. Strongly
FT increased catalytic activity; when associated with S-480 or
FT I-482 or S-366 and I-482 or S-480 and I-482."
FT /evidence="ECO:0000269|PubMed:17715131"
SQ SEQUENCE 502 AA; 56788 MW; 424EA8D44BB8958C CRC64;
MQFFSLVSIF LFLSFLFLLR KWKNSNSQSK KLPPGPWKLP LLGSMLHMVG GLPHHVLRDL
AKKYGPLMHL QLGEVSAVVV TSPDMAKEVL KTHDIAFASR PKLLAPEIVC YNRSDIAFCP
YGDYWRQMRK ICVLEVLSAK NVRSFSSIRR DEVLRLVNFV RSSTSEPVNF TERLFLFTSS
MTCRSAFGKV FKEQETFIQL IKEVIGLAGG FDVADIFPSL KFLHVLTGME GKIMKAHHKV
DAIVEDVINE HKKNLAMGKT NGALGGEDLI DVLLRLMNDG GLQFPITNDN IKAIIFDMFA
AGTETSSSTL VWAMVQMMRN PTILAKAQAE VREAFKGKET FDENDVEELK YLKLVIKETL
RLHPPVPLLV PRECREETEI NGYTIPVKTK VMVNVWALGR DPKYWDDADN FKPERFEQCS
VDFIGNNFEY LPFGGGRRIC PGISFGLANV YLPLAQLLYH FDWKLPTGME PKDLDLTELV
GVTAARKSDL MLVATPYQPS RE
