CY079_POSPM
ID CY079_POSPM Reviewed; 567 AA.
AC F1SY75;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Cytochrome P450 monooxygenase 79 {ECO:0000303|PubMed:21938516};
DE EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN Name=CYP079 {ECO:0000303|PubMed:21938516};
GN Synonyms=CYP5027B4v1 {ECO:0000303|PubMed:21938516};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Dacryobolaceae; Postia.
OX NCBI_TaxID=561896;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=ATCC 44394 / Madison 698-R;
RX PubMed=21938516; DOI=10.1007/s00203-011-0753-2;
RA Ide M., Ichinose H., Wariishi H.;
RT "Molecular identification and functional characterization of cytochrome
RT P450 monooxygenases from the brown-rot basidiomycete Postia placenta.";
RL Arch. Microbiol. 194:243-253(2012).
CC -!- FUNCTION: Cytochrome P450 monooxygenase that is able to use
CC dehydroabietic acid as a substrate for oxidation.
CC {ECO:0000269|PubMed:21938516}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB573286; BAK09419.1; -; mRNA.
DR AlphaFoldDB; F1SY75; -.
DR SMR; F1SY75; -.
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; 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.
PE 1: Evidence at protein level;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..567
FT /note="Cytochrome P450 monooxygenase 79"
FT /id="PRO_0000451363"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 475
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:P04798"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 567 AA; 64219 MW; FE264203051B4098 CRC64;
MAVSTNELAI LAIVLLVTAV VFYTKGTRRA PLPPGPRGIP FLGNLFQFNV MRPYPQYLKW
AQKYGPVFSI KLGSQRIIVL STSEAADELF VTRSKLYSSH ESPHVGFDLV SDQQRMVFMP
YSREWKIVRK NVHGILGPGP SKQMRKMQDL ECRIMLHDLL CHGDTSIVED FVEGPHGKVP
ERHWFSIIRR YTTSLMMTLV YGRRIHRIVD NPELHQVYEM MSNMTHVSQP GRYLVDALPI
LRWLPDIMAP WRAEGKRMHE WEMGFWGKLF ADSRTAFLNG TGLNGFVQSY LSARAEAGLE
DLPGKGATED GAGWMRDKLI TYTAVSIIEA GSDTTSTAVF SFVLLMLSNP DALRRAKEEM
GAVVGSSRMP DWEDEDRLPW LTACIKETLR CAPPLPLGIP HKADEDDVYN GYLIPKGSTV
IGNIWAIHMD PVRYPDPTAF KPERFYNPDG KLNWASGPDT HNRDHYIFGW GRRFCSGKYL
AEASMFIVLS RLIWGFDFYA ASDPQTGKVK LPDVNDVDTF TDGLVTAPKI YPVGFKPRSE
KHAEMIKASY RDVQNDWQSM GLAGDER