ID A0A395NXH6_TRIAR Unreviewed; 499 AA.
AC A0A395NXH6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cytochrome p450 6a1 {ECO:0000313|EMBL:RFU80822.1};
GN ORFNames=TARUN_1387 {ECO:0000313|EMBL:RFU80822.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU80822.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU80822.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU80822.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU80822.1}.
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DR EMBL; PXOA01000087; RFU80822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NXH6; -.
DR STRING; 490622.A0A395NXH6; -.
DR Proteomes; UP000266272; 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; 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; 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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW Reference proteome {ECO:0000313|Proteomes:UP000266272}.
FT BINDING 437
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 499 AA; 55877 MW; C87FF3B14A1E4DF3 CRC64;
MVSLVATFAS PQNWPASALL LVATLAVLLV SRLLKRADLP PGASWTEKGL PFIGSIPFFT
KRGDFLLEGT KRSPNGYFNF YYGSYPIIAL SGEAARTAYF TTRGLDLNAG FRKLFSAGPD
IDHLLGCNMS AYFVALFKRL TGRDYLVHCI PYLTKDAHAS FTAVDTSVPM DPFLVLYDLI
YKMTHRTVGC HDVAEDPVLQ EKTMRYYEKV DRSSAMEVMF PSLPTPTKLS KLWAGAKLHM
LFGDIIKERR RTGRRKEDTM QILMDKGESD LLSSAFIIGA LFAGLINTGV QSAWILSYLA
YNSEWYAKIQ GEVDAAVAKH RTSDDQTPVD VLQSLTLEDW EAEFPFLDLG VRESIRLNLM
GASIRQNTSG KDIVLGDTGV VVPKDAFAVY HVADIHLNDS VYTDPMRWDP GRYLPEREED
KKDQHGYIGW GTGLHPCLGM RIAKLELFVS TAVFFATFNF KAVDKNGNTR TEPLPGYDNN
ALAAKRILGM MYLKCERRF
//
