ID S7ZZJ0_PENO1 Unreviewed; 515 AA.
AC S7ZZJ0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PDE_09230 {ECO:0000313|EMBL:EPS34266.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS34266.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS34266.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617}.
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DR EMBL; KB644415; EPS34266.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZZJ0; -.
DR STRING; 933388.S7ZZJ0; -.
DR eggNOG; KOG0684; Eukaryota.
DR HOGENOM; CLU_033574_2_0_1; -.
DR OrthoDB; 3685322at2759; -.
DR PhylomeDB; S7ZZJ0; -.
DR Proteomes; UP000019376; 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 GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd00302; cytochrome_P450; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46206; CYTOCHROME P450; 1.
DR PANTHER; PTHR46206:SF5; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 452
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:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 515 AA; 58359 MW; 18B5D66367BE179F CRC64;
MDSTYADRFH DLDLPIKVAA TGLLATVTTF LAYIVFLSYT PHVDKNSPQF TSNTVPLVGS
WSFFTQKWAF WKDCVAKSKT GHFSFWLGKY HVVGVSGAAA RKLFLDNPQF DFVRGATLVG
HGPDLVPPLH EIFHVNFQNG RTYFQRRLLD VQKSEQLEKR VPGVTKDARM TFEALRQSAS
SIMNPTDTCY RLVVQQASRV VCSDEIADAP AVLAKTQSVL SLLMHTSSIH AVALPYLPWL
SKLKRRWGRY GLSKIVTPIV QRRRQKDAPR KDDMVQYMLD RGDSPEWMVN FFISTLFISS
ANAGYLSGAM LNILAHHPDW QSRIYREIAT VAETHASNRH APLVDQLDSI PLEAWETHFP
SIDLCFKEAI RMWVAFPMIR LNMASHAVPI PGTNEVVPAG SFAAYNTTEV HFNPELYPDP
YKYDPNRFSE GREEFKKEAY GFVGWGQGRH PCLGMRWARV QLNIILAYAL AMYEWSGCDE
NGQPSSHFDR KTDLNAPGPS LPVGLYCKYV PREKV
//
