ID   CYPU6_GANLU             Reviewed;         509 AA.
AC   A0A346B546;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Cytochrome P450 monooxygenase CYP512U6 {ECO:0000303|PubMed:30077898};
DE            EC=1.-.-.- {ECO:0000269|PubMed:30077898};
GN   Name=CYP512U6 {ECO:0000303|PubMed:30077898};
OS   Ganoderma lucidum (Ling zhi medicinal fungus) (Bracket fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=5315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=30077898; DOI=10.1016/j.phytochem.2018.07.009;
RA   Yang C., Li W., Li C., Zhou Z., Xiao Y., Yan X.;
RT   "Metabolism of ganoderic acids by a Ganoderma lucidum cytochrome P450 and
RT   the 3-keto sterol reductase ERG27 from yeast.";
RL   Phytochemistry 155:83-92(2018).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase that hydroxylates the ganoderic
CC       acids DM and TR at the C-23 position to produce hainanic acid A and
CC       ganoderic acid Jc, respectively. {ECO:0000269|PubMed:30077898}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ganoderate DM + O2 + reduced [NADPH--hemoprotein reductase] =
CC         H(+) + H2O + hainanate A + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:68732, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:178026,
CC         ChEBI:CHEBI:178027; Evidence={ECO:0000269|PubMed:30077898};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68733;
CC         Evidence={ECO:0000269|PubMed:30077898};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ganoderate TR + O2 + reduced [NADPH--hemoprotein reductase] =
CC         ganoderate Jc + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:68736, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:178028,
CC         ChEBI:CHEBI:178029; Evidence={ECO:0000269|PubMed:30077898};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68737;
CC         Evidence={ECO:0000269|PubMed:30077898};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:30077898}.
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; MH431572; AXL48364.1; -; mRNA.
DR   UniPathway; UPA00213; -.
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   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
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..509
FT                   /note="Cytochrome P450 monooxygenase CYP512U6"
FT                   /id="PRO_0000454389"
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         446
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   509 AA;  56753 MW;  AE55C82EDB2581DF CRC64;
     MLALMDDIQS AVFACVAVVI AIYAVRWYTD PINSIPTVGG SSLPGLSLLT AWRTVHNCRE
     VLTAGYRKYP DSVFKIAMFD SWLVIASGRN MIEEVRKRHD ELSTTLGIQE ALRSRYIRDR
     QVMTDEYHVR VVKEKMSGRT LQAMLPDVIE EVSIAVKDHI ATQGSGWTSL EVVPAMQKVI
     FQVNNRAFVG PVLCRSKEYL NVAIDFSEHT FKWSAILSVT PEFVRRIIAP FINEAKNDTR
     RAVPLLRPII EERMKAQADL GEGWHDKPND ILQFVLDKAI PKEESMFLIV HRLLIVNHAA
     SGNSVNAITY VLYHLAENPD ILQACREEAE AKIAADGWTS TALANMWRLD SILRETLRYH
     GTALVSMNRL ATKDVVLSDG TRLPKGTFMQ AAAYPLHRDG ALVENAHTFD PFRYARMRDA
     DGEGLKHQAS TTSPEYIPFG HGQHACPGRY FAAYVLKAIL AHLIVNYDLK LGGDGSRPPI
     RYVLSAVLPP PGGCVLLKER GEGSTTTTG