ID   CY197_POSPM             Reviewed;         545 AA.
AC   F1SYG6;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Cytochrome P450 monooxygenase 197 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP197 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5139D6 {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 carbazole
CC       as a substrate for oxidation. {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; AB573377; BAK09510.1; -; mRNA.
DR   AlphaFoldDB; F1SYG6; -.
DR   SMR; F1SYG6; -.
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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
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..545
FT                   /note="Cytochrome P450 monooxygenase 197"
FT                   /id="PRO_0000451374"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         481
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        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   545 AA;  61281 MW;  CF604A41E56163CE CRC64;
     MVFVTTTNVL LSMSGAIAAI VLWKVISILR APYTSALRNL PGPPSPSWPL GHLKMMFSAE
     DSAALYESWV ERHGTTFKYN GWAGTYRLFT ADTRAVNYIQ SHSNDYWKPE ISRFSLIQIL
     GHGLLSVEGD RHRQQRRVMN PAFGPAQIRG LTEIFVEKAH KLCEFWRNEL SKNGEPGRIE
     VLNGLSKMTL DVIGLAGFNY DFNSLNVDGK PNELNEAFNV LFRSLDGFAI LPVLQAVFPP
     LRLLPDRRSR RIASAVKVMR RIGMELISNK KAEIVAAAIS DQKEKNKLQS RDLLTLLLKS
     NLSRDNPESQ RLSDKDVLAQ VPTFLIAGHE TTSNAVAWCL YALTQNSEIQ QKLRDELWSV
     PTEDPTMDEL NELPYLEAVV RETMRVHAPV PATERVAIKD DVILLNTPYI DIRGQVQDSV
     RVRKGDHIFI PIIAMNKSKA LWGEDAFEFK PERWESIPDA VQTIPGVWAN MMSFLGGAHS
     CIGFRFSVVE MKALVFALVR SFEFELAVPA GQLTAKTIGV QRPAVRGEQN QGCQLPLLIK
     VYKRN