ID   CY113_POSPM             Reviewed;         495 AA.
AC   F1SYA2;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Cytochrome P450 monooxygenase 113 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP113 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5152A4 {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 4-
CC       ethoxybenzoic 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; AB573313; BAK09446.1; -; mRNA.
DR   AlphaFoldDB; F1SYA2; -.
DR   SMR; F1SYA2; -.
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..495
FT                   /note="Cytochrome P450 monooxygenase 113"
FT                   /id="PRO_0000451358"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         428
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   495 AA;  55496 MW;  B5F42CF857260DD6 CRC64;
     MFLQIAACFT VIGLLYGLVS NLQQNRRLAA SLPPGPPGHW LFGNVPPKNF PFIRFAELTE
     IYGPVFTLRF GRRIVCVVGR HQAAVDILVK HSAETTDRPR AIAASEMLSQ GFRILMTPAG
     ERLKKYRRAF HTCLQPSAAA TYKPIQYNHA KNYILDCLHD GKCHLEHGRR YAASVVMYIG
     YGKTTPTSYS DPEVQEVNKC LGRLSEVIKP GAYLVDTYPI LKHIPGYASH LWRYGREELA
     LYTRQANAVR KQLEKDEAQP SFAAYLIENQ ERLGLSNDEL AYLSGAIFGA GSDTTAAAIA
     VMTMAAACYP ETQARVQAQL DEVVGSDRAP TFEDEEMLPE VTAFVLEVYR WRPVSAGGVP
     HRSTKDIVWN GYVIPKGTEI IGNLWAIGRD PELFPDAEEF RPQRWLNENG RIRDDLKYPV
     FGFGRRVCVG QHVADQSLFI NTALALWAFK ISQDPAKPID VLAFTDTANI RPLPFTLRFE
     PRVKDIEAVL EAHLD