CY088_POSPM
ID CY088_POSPM Reviewed; 495 AA.
AC F1SY82;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Cytochrome P450 monooxygenase 88 {ECO:0000303|PubMed:21938516};
DE EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN Name=CYP088 {ECO:0000303|PubMed:21938516};
GN Synonyms=CYP5152A3v2 {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 4-
CC ethoxybenzoic acid as a substrate 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; AB573293; BAK09426.1; -; mRNA.
DR AlphaFoldDB; F1SY82; -.
DR SMR; F1SY82; -.
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..495
FT /note="Cytochrome P450 monooxygenase 88"
FT /id="PRO_0000451357"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 428
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 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 495 AA; 54876 MW; A17438BB3B833C0E CRC64;
MFLQIVTSVL ATGLLYALIS VLQQNRTLSA SLPPGPPGHW LFGNAPPKAF PYRHFAELTE
TYGPVFTLRF GRRIVCVIGR YQAAVDILMK HSAETSDRPR SVAANEIMSK GHRVLMTPAG
ERLKKYRRAL HAFLQPSSSA TYKPMQYKNA KNYVLDCLHD GGHHLDHGRK YAASVVMSVA
YGKTTPTSYS DPEVLQINKS LARLGAALKP GAYLVDTYPI LKYCPGYASH LRRYREEELA
LITKQANAVR ELLAKGEAPP SFTAYLIENQ ERLGISDDEL AYLSGAIFGA GSDTTAAALG
IMTMAAACYP EAQARVQAQL DEVVGRDRAP TFEDEDLLPE VTAFVLEAYR WRPVSAGGFS
HRATKDVVWN GYVIPAGAEI IGNHWAISRD PEVYPNPEDF KPARWLNEHG RVRNDLKFTN
FGFGRRVCVG QHVADQSLFI NTALVLWAFI ISQDAQCPID TYAFTDTANV HPLPFSLHFE
PRVKDMEAML GAQAE