CY110_POSPM
ID CY110_POSPM Reviewed; 498 AA.
AC F1SY99;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Cytochrome P450 monooxygenase 110 {ECO:0000303|PubMed:21938516};
DE EC=1.-.-.- {ECO:0000269|PubMed:21938516};
GN Name=CYP110 {ECO:0000303|PubMed:21938516};
GN Synonyms=CYP512N6v2 {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
CC dehydroabietic acid and testosterone as substrates for oxidation,
CC suggesting that the natural substrate(s) may be structurally related to
CC steroid compounds. {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}.
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; AB573310; BAK09443.1; -; mRNA.
DR AlphaFoldDB; F1SY99; -.
DR SMR; F1SY99; -.
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..498
FT /note="Cytochrome P450 monooxygenase 110"
FT /id="PRO_0000451361"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 440
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 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 498 AA; 56594 MW; 568B69F3CB5FEF49 CRC64;
MEDKAQYVFA LLGILATLYF VRWSTDPLRH IPAIGPSAPI VSYLSAYRYC RNAQSILQEG
YHKYKVFRVS LVDRWVVVVS GADMNEELRK VPDTHVSFQE AADDLIQLKY TIAPDVNEHP
IHTPVIRGPL TRNLGALFPD VVDEINVAFP ELMPPAAKRG DWVAVSVRDT MGRIVSRASN
RIFVGLPLCR NPDYLKTVVE FAFSVAKSRT IINAAPAVFR PIVGHFLPWA KRAVRNAGVH
VKPLIRLRVS KMQDAGDDQT DKSCDYLMWL IEEAQKTKQN LDIVVQGILV SNFAAIHTSS
NSITHSLLNL AAYPQHVQPL REEIEGIIKE YGWTKEAIGK MWKLDSFMRE SQRLSGISGI
SVMRKVLQDI TLSDGTYLPK GTLVVAAAFA THTDERYYEN PEVFEPFRFY DMRTENDALR
KQYVNTSREF ITFGHGKHAC PGRFFAVNEL KAMMAYIILH YDVKLEEGVS RPENVWIWHN
ISPASTKVLF RERQSKVQ