ID   CY103_POSPM             Reviewed;         500 AA.
AC   F1SY95;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Cytochrome P450 monooxygenase 103 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000305|PubMed:21938516};
GN   Name=CYP103 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP512P1v2 {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       testosterone 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; AB573306; BAK09439.1; -; mRNA.
DR   AlphaFoldDB; F1SY95; -.
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   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..500
FT                   /note="Cytochrome P450 monooxygenase 103"
FT                   /id="PRO_0000451366"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         441
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        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   500 AA;  56570 MW;  60FDDE14DAB4369C CRC64;
     MASTPLLYVL VIILSAVYLL RRRSNPLYAI PAVGPSLPLL SYIGALRFTR HAHEMLQEGY
     IKYKGSAFRL AQLDRWVVVL CGPKMNEELQ RMPDDQVSFL DAAEDLVQTK YTIAKNVIEN
     PIHISVMRGP LTRNLAPLLL DVIDEINIGV EEHIPTRGDE WVSVPGLATM TQIVSRASNR
     VFVGLPMCRD PEYFKIISNF PRDVAKGRFI LSITPTFLKP IIGPLLPWSR RTVRQYSALM
     KPIIEERQRL LLEHRDPHDP DRPNDFMTWL IEEGRAVDQP VDLLVNALLS SNFVAIHTSS
     ISVTHALYNL AAYPEYQQPV RDELVEVIKA EGWTKQAFGK MWKLDSFMRE SQRMFGISAI
     SVIRKALKDV TLSNGTVIPA GTLIAVAAEG THYDEGSYDN PYIFNPFRFS DMREDEGERI
     KHQYVSTSSE YVSFGHGKHA CPGRFFASNE LKAILSRLIL DFDMKFGGDG HRPPNQWFGS
     SIIPSQTANV MFRKRPDAGL