CY045_POSPM
ID CY045_POSPM Reviewed; 529 AA.
AC F1SY52;
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 45 {ECO:0000303|PubMed:21938516};
DE EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN Name=CYP045 {ECO:0000303|PubMed:21938516};
GN Synonyms=CYP251 {ECO:0000303|PubMed:21938516},
GN CYP5350B3v1 {ECO:0000303|PubMed:21938516},
GN CYP5350B3v2 {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 trans-
CC stilbene 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; AB573263; BAK09396.1; -; mRNA.
DR EMBL; AB623253; BAK20189.1; -; mRNA.
DR AlphaFoldDB; F1SY52; -.
DR SMR; F1SY52; -.
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 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..529
FT /note="Cytochrome P450 monooxygenase 45"
FT /id="PRO_0000451397"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 454
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 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 529 AA; 58964 MW; E226F22C358123F8 CRC64;
MHSVLAQAAS GALSFELRLG QSSVLTICIL ALLTFVLREI VLYFTRHSMP PGPFRWPLIG
NALQLPQDHP WVKYTEWAKM YGPLMQLDVL GQHMLVITSA QTARDLMEKR SSIYSDRPHL
VMAGDLAGFG DTLILQNYGE EFRYQRKLVS HSFSPSVIHR YYDLQEAAAR RLVLAIIEDP
DSLENSTRLH IASIILRMTY GYTVKGVDDP LFTTGIAVIN GFSEATRPGA WPVDFVPILQ
YVPHWVPGFV FTRKAREWRG VLERAMWAPY HWCKENYARD AAHGLCLCGS ILAAEGSQLS
SDQEWLFVNA AVTVMGGGLD TNISTILSFV LAMLRFPEVQ KKAQAEIDAV IGPNRLPLIS
DRHSLPYVRS VVTEVYRWIP AVPLGIPHAL RQDDHYDGLF LSKGSVVVPN VWGMLHDPSI
YPAPHEFKPE RYGGLDAEMT KVTDIAFGFG RRACPGFYFA EGTIFAIVAT VLAICDVVPT
VDEHGQEVIP EVSLTSGAIV SPENVKCAFR PRSGRVKDIL VEAVETEQE