ID S3CP08_GLAL2 Unreviewed; 468 AA.
AC S3CP08;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:EPE27455.1};
GN ORFNames=GLAREA_04246 {ECO:0000313|EMBL:EPE27455.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE27455.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE27455.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KE145369; EPE27455.1; -; Genomic_DNA.
DR RefSeq; XP_008084814.1; XM_008086623.1.
DR AlphaFoldDB; S3CP08; -.
DR STRING; 1116229.S3CP08; -.
DR GeneID; 19463301; -.
DR KEGG; glz:GLAREA_04246; -.
DR eggNOG; KOG0159; Eukaryota.
DR HOGENOM; CLU_001570_14_0_1; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
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 CDD; cd11060; CYP57A1-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF175; CYTOCHROME P450 MONOOXYGENASE PKFB; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602403-1,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT BINDING 408
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 468 AA; 52948 MW; 99285D8E3047CE41 CRC64;
MLWVPTKRAH LILQEMHEKY GEVVRIGPNM VSFCNPEVIP IVYPTRQGFP KSDFYATLRP
YTRGGGALQA VFNVTDEKVH KQLKSPIAPI FSPTSATLFE PLVDDVLQCL LNQLDTRFAA
NGEVLNLGAW VQFFAFDVMG TMTFSKRYGF LDNGRDVGGM LSTIVDFMRS AAPMTQVPWL
DRIMRKNLIA DTFRQIFNQT ASLSILGFVG DAIKEKRASL ANGTDKVGDK TSTKKDFLSR
YIELQESSAE IPHWAPTAWT FSNVIAGSDS VGSLMRTIMF CLLSYPNTLD KLYNELLSAN
LSRPFPAYKE LRNLPYLDAC IQEGSRIHPP FALPFERVVP EGGITIIGHF LPAGTVVGGS
PYVVNRHKSF FGQDAEFWRP ERWLEKDDAH KRRLEQGVLT FGAGRRVCLG KHIGILEIKK
LIPFLILNYD IRIIDREKFQ VENSWFLFQT GLYAQLQKRP ESVINPQL
//