ID B8M886_TALSN Unreviewed; 544 AA.
AC B8M886;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE SubName: Full=Cytochrome P450, putative {ECO:0000313|EMBL:EED20399.1};
GN ORFNames=TSTA_036250 {ECO:0000313|EMBL:EED20399.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED20399.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962654; EED20399.1; -; Genomic_DNA.
DR RefSeq; XP_002480833.1; XM_002480788.1.
DR AlphaFoldDB; B8M886; -.
DR STRING; 441959.B8M886; -.
DR GeneID; 8101896; -.
DR VEuPathDB; FungiDB:TSTA_036250; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_018012_3_0_1; -.
DR InParanoid; B8M886; -.
DR OMA; TENHNIW; -.
DR OrthoDB; 2289306at2759; -.
DR PhylomeDB; B8M886; -.
DR Proteomes; UP000001745; 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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11040; CYP7_CYP8-like; 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; PTHR24304:SF2; 24-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE; 1.
DR PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 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|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
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:UP000001745}.
FT BINDING 478
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 544 AA; 61131 MW; 5B444EC01504E3B0 CRC64;
MTVTSFPSIA SRTFPQAHSI EMISELLSSV LGGSQHLLIL LPTWTAALWI LWYCWKFILS
PHFYKDEPPI YPYYIPFIGH LRSFIQDAGS LVKKAESCFG EGKLFGVQIA GKKLYIITSA
EGTKEFYRNT TALDFTAFQL DTLKQFGMSP AGCKLMSKHI QGRTNGRDRI NIDLIVDVHH
RNLHSSANLG QIASPVAEYI SNALRLETLP EQCIRFPGPR TEGKVVSLYT LCEEVILRAN
ITGFWGNDLL DIAPDLVSTT STLDRRFHNL LLRIPRLLEP EVYNLRDKVL DYFDRYMDIP
MKARTSLSPL IKELEQTSRD LGLSQRDIAV YHLAWLLASN NNIHAACFWV LAHLAESPDL
ANKVREETAG IARNALSFSP AEALKDNQLP CLMALWREVL RFYGGPHTSG RHVQEDTVFT
GKRLRRGASL LVATSTLQRD KAVWGADADE FVPNRFLRSP YLAKVANYRP FGGGISHCSG
QHLAFVEMAM VVACLLDRFD MQIVPGVEET AFPQPFKAAP LLGIMHVREG DDKLVMLVPR
LTGR
//
