CY075_POSPM
ID CY075_POSPM Reviewed; 613 AA.
AC F1SY74;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Cytochrome P450 monooxygenase 75 {ECO:0000303|PubMed:21938516};
DE EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN Name=CYP075 {ECO:0000303|PubMed:21938516};
GN Synonyms=CYP63A6v1 {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 and 3,5,4'-trimethoxy-trans-stilbene 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}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB573285; BAK09418.1; -; mRNA.
DR AlphaFoldDB; F1SY74; -.
DR SMR; F1SY74; -.
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 Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..613
FT /note="Cytochrome P450 monooxygenase 75"
FT /id="PRO_0000451372"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 526
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 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 613 AA; 69844 MW; 7C91E3589D99FF73 CRC64;
MALPPGVPFL IRVSLILAFA PVCVVIVANF IWRHTDVALP TWPVTLLSVA STPLTILVRV
WYRQWKYQRA AARLGAIMPP RWVGKKLGNL DILKEMLQTM QSGYIADFAW KLFNNLGNTV
QMNVLGGTAY LTCDPNIIKS VLATDFNNFE KGDLFKQEMA SVLGTGVFNA DGDMWKWHRA
MTRPFFSRDR ISHFELFDRR SEQAVAKMTE RFHSGYAVDF QDLISRFTLD SATEFLFGSC
VNSLHSPLPY PHNQHPTPFS HPSSKSLASN PSRAEAVASA FMRAQIVLAE RVAMGAIWPL
LEMRKSRTGE HMRIIDEYLD PILKDALRRK EDMANIGAGI HDDKESSDTD GETLLDHLVR
LTSDPVVLHD EVLNILIAGR DTTAGTLTFV VYFLCMYPDV FNRLRAEVLE KVGPNARPTY
ADIKEMRYLR AVINETLRLY PVVPFNIRWS IHEGTLPNPD PNGKPFYLPP KTPVTYTVFA
MHRRKEYWGP DADEFDPDRF LDDRVAKYLT KNPFIFLPFN AGPRICLGQQ FAYNEMSFFL
IKLMQHFSAM ELAPEAAPPE SLPPAEWAVT GWGRKRIERF WPKSHLTLYS NGGMWVKMVE
ADDFDKDDRD VGI