ID K5WE27_PHACS Unreviewed; 554 AA.
AC K5WE27;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHACADRAFT_254974 {ECO:0000313|EMBL:EKM57284.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM57284.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM57284.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM57284.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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DR EMBL; JH930471; EKM57284.1; -; Genomic_DNA.
DR RefSeq; XP_007395100.1; XM_007395038.1.
DR AlphaFoldDB; K5WE27; -.
DR STRING; 650164.K5WE27; -.
DR GeneID; 18916187; -.
DR KEGG; pco:PHACADRAFT_254974; -.
DR HOGENOM; CLU_001570_14_10_1; -.
DR InParanoid; K5WE27; -.
DR OrthoDB; 2117278at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0016020; C: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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11061; CYP67-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF242; CYTOCHROME P450 MONOOXYGENASE ATNE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 554 AA; 61912 MW; BEED7B4D1F5343FD CRC64;
MPDTTDPKLL VCSASFACYL VYKYFEPNNL SAHVVLLLGV PALLVGRLSP QLSFLQQAGA
VIFYWSLILV FTATYRLSPF HPLAKYPGPT LGKLSRIYVA YFNGRGDLHR VIRDWHDRYG
DVVRIGPNEL SFCRADALQP IYVAKSMQKG PYYDTRTGLE NITTLDGVRD FSVHGARRKP
WVKAMGISAL KGYEPILQTK ILELVEVLSK RQKETIDISH WMNLFGFDLI GHVAFGHEFG
MLKAGEDDDG LMRRVEDGVY ATAVLSQTPW ILPFIRRLPP AVKAIRDMRH MGATLAQGRT
KNGSASKDLF YFLTEDETAA ESGATLDEII ADGILALVAG SDTTATVLSH LCYFMLRHPE
CAERLHKEID ATFPPGEDPL DFSRHADMPY LNACINETLR LLPAVLGGLQ RIVKRGSSGA
TIGPHVVPEG TQVSVHTFSL HRDPREFAPL PDVFWPDRWL AQDTYVLPSG AAVDKAHVTT
NRAAFVPFSV GPQNCAGRAL AMIEMRAVVC AVMHKFELRR AEEYDLDRWE RDVMDAYISL
RGKLPVILEQ RQGR
//
