CY081_POSPM
ID CY081_POSPM Reviewed; 547 AA.
AC F1SY77;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Cytochrome P450 monooxygenase 81 {ECO:0000303|PubMed:21938516};
DE EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN Name=CYP081 {ECO:0000303|PubMed:21938516};
GN Synonyms=CYP5150D18 {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}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB573288; BAK09421.1; -; mRNA.
DR AlphaFoldDB; F1SY77; -.
DR SMR; F1SY77; -.
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..547
FT /note="Cytochrome P450 monooxygenase 81"
FT /id="PRO_0000451364"
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 483
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 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 547 AA; 61636 MW; 08AFBB085B39E0BF CRC64;
MSTDNIPTQL GIAGAVAVLL FLLRRWSSRS TLRNIPGPPP QSQWTGNLKQ WFARDGADFQ
RDVSFNYGPV AKIHGFLGRP ILYVADPKAL QTILVKEEQV YQETKAFFAM TYLLFGPGLL
ATAGEKHRKQ RKLLNPVFSI KHMRHMLPIF YGVLHKVRDA ITMRVSDGPQ EIDMLKWMGR
TALELIGQGG LGYSFDKLVE DGDNEYGRAL KHLQPTLQRI NVLRRLIPYV YKLGPAWFRR
MVMHYFPLGQ VRDAKEIVDT MQRCSSEIFA SKKIALARGD EAVMKQVGEG KDIMSILMKA
NSMASEADRI PEEELVAQMS TFLFAATDTT SNTLARILQQ LAIHPDTQQK LREEILAANA
EEYMAYDDLD ALPLLDGVCR ETLRVFPGVT NLARTPTQDT ILPLSEPVVG TDGTVMREIL
VPRGTEILIG IQGSNGRKER WGEDSYEWKP ERWLSPLPKT VTENPVPGVY SNLMTFMAGR
RACIGFKFSE MEMKVVLAVL LSNFTFELTD KPIQWNISGV RYPTVGKDSN VAQLPLKVGL
YKKPTLQ