ID   CY136_POSPM             Reviewed;         529 AA.
AC   F1SYC2;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Cytochrome P450 monooxygenase 136 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP136 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5348E1 {ECO:0000303|PubMed:30105900},
GN   CYP5348E1v1 {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], AND IDENTIFICATION.
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).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 44394 / Madison 698-R;
RX   PubMed=30105900; DOI=10.1111/1751-7915.13304;
RA   Ichinose H., Kitaoka T.;
RT   "Insight into metabolic diversity of the brown-rot basidiomycete Postia
RT   placenta responsible for sesquiterpene biosynthesis: semi-comprehensive
RT   screening of cytochrome P450 monooxygenase involved in protoilludene
RT   metabolism.";
RL   Microb. Biotechnol. 11:952-965(2018).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase that is able to use delta(6)-
CC       protoilludene as a substrate to produce delta(6)-protoilludene-5-ol.
CC       {ECO:0000269|PubMed:30105900}.
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; AB573333; BAK09466.1; -; mRNA.
DR   AlphaFoldDB; F1SYC2; -.
DR   SMR; F1SYC2; -.
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   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..529
FT                   /note="Cytochrome P450 monooxygenase 136"
FT                   /id="PRO_0000451348"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         447
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"
SQ   SEQUENCE   529 AA;  59509 MW;  C0C03A4E401EA005 CRC64;
     MQLPVQLSSP LALAVLSIAT CQLALVWWYQ RKRTNPLPPG PSALPFLGNA HQIPLQYPER
     IFSQWARTYG GVMYLRLFKK SVLILDSVKA AQDLMDKRGA KFSDRPQLTL ITDVFAFKPM
     MFTMPYGDLW RRHRKWYQAS LESKAALDTY NAVQEMETCT LLSALVSDSE HFADQVKRFT
     GAILLEIVYG HAVTSVKDDL IRLSDEMMTQ AVSAGSLVAT LLDFFPFLMH IPEWFPGGGF
     KREGARVRHL MRQLLDVPFN EVQQAMLEGS GKACLTTYML EEQAEHGDLT PDDVDNIKGA
     ATLLFIAGTD TTITTLLTFF LAMVLHPEVV HKAQAEIDRV VGRTRLPSLM DRDALPYLDQ
     VLKEVYRWNP PVPLGIPHQV RDDDVYNGRH IPGGSMVVSN IWSMSRDPDT YEDADRFWPE
     RYEGKSSDEL ARSDPRRIVY GFGRRLCPGR FLADSSIWLA AARVIATLDI RKVLDAEGKE
     MTPSAEFISG AVSHPKPFSL DILPRDEVAA KLIAQLDPNH LFSVQGEAI