ID   CY128_POSPM             Reviewed;         547 AA.
AC   F1SYB6;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Cytochrome P450 monooxygenase 128 {ECO:0000303|PubMed:21938516};
DE            EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN   Name=CYP128 {ECO:0000303|PubMed:21938516};
GN   Synonyms=CYP5139D2 {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 7-
CC       ethoxycoumarin and testosterone as substrates 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; AB573327; BAK09460.1; -; mRNA.
DR   AlphaFoldDB; F1SYB6; -.
DR   SMR; F1SYB6; -.
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..547
FT                   /note="Cytochrome P450 monooxygenase 128"
FT                   /id="PRO_0000451353"
FT   TRANSMEM        9..25
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        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   547 AA;  61880 MW;  5CABB7F15515D107 CRC64;
     MLSLTAHDIP WAAGATLLAW AAYKIGRILL LPYTSPLRGL PGPPASSWLF GNVNELMGTE
     DFALYSEWLE KYGPTMKLNS WFKIPKLFTI DTRAMNYVLS HSQEYPKPER SRHNLVQILG
     NGLVVAEGEL HRRERRIMNP AFGPAQIREL TEIFVEKSQQ LRDIWWNDVA IRGGSARIDI
     QSGLTKMTLD VIGLAGFNYE FNALNPDGKP NELNAAFEVM FEYLSNLRKS YWLIIRSRFP
     ILRCIPDGYS RRTAAAHKVT RRIGLQLIAE KKAALKQMAQ SGEKTAGTAL KSRDLLTLLI
     KANTSPDIPE DQRLSDEDVL AQVPTFLVAG HETTSNATTW CLYALAQRLD VQRKLREELR
     EVPVDNPSMD QLNALPYLDA VIRETMRLYP PVVAGIRIAS KDDEIPLAVP YMDAHGRMHD
     TVRIDKGTTF PIPILGVNMS KALWGEDARE FKPERWESVP EAVQPIPGVW SNLMTFIGGP
     RACIGYRFSL VEMKALIFTL VRAFEFEMAV PIEDITRKIG LVQRPFVRSE MEKGTQMPLI
     VKQHVRL