ID A0A084QC67_STAC4 Unreviewed; 536 AA.
AC A0A084QC67;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=sterol 22-desaturase {ECO:0000256|ARBA:ARBA00039038};
DE EC=1.14.19.41 {ECO:0000256|ARBA:ARBA00039038};
GN ORFNames=S40285_03986 {ECO:0000313|EMBL:KFA61552.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA61552.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA61552.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA61552.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000256|ARBA:ARBA00004685}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KL660849; KFA61552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QC67; -.
DR STRING; 1283841.A0A084QC67; -.
DR HOGENOM; CLU_023517_0_0_1; -.
DR InParanoid; A0A084QC67; -.
DR OMA; IMDAWIL; -.
DR OrthoDB; 5393233at2759; -.
DR Proteomes; UP000028524; 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; cd11082; CYP61_CYP710; 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; PTHR24286:SF228; C-22 STEROL DESATURASE ERG5; 1.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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|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 ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT BINDING 481
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 536 AA; 60645 MW; 370586C4DA01DD84 CRC64;
MDATNSSTVF TSVLPSFGSY AGVNLPPQVD VVLDTLSRLS GWTIALTVLA VLVAYDQISY
ILNKGSIAGD SWKVPFIGPF LDSMNPKFDG YYAKWVSGPL SCVSVFHKFV VIASTRDMAR
KVLLSPTYVK PCVVDVAHKL LGADNWVFLD GKPHHDFRKG LNILFTRNAL ENYLPGQQEV
YNRFFKRFVN TTEKAGGKPV PFMFEFRDLM CAVSCRTFVG HYISDETVQR IAEDYYLITK
ALELVNFPII LPFTNAWYGK KTCDMVMAEF TNCAAKSKVR MQAGGDVTCV MDAWILQMVK
SEEWRQAVEK GEGEGLEKPA PYLRMFNDYE IAQTIFTFLF ASQDAACSAT TWLFQTMAQR
PDVLDRVREE NLAVRNGDAK ADISMDQLES LKYTRAVVRE LLRYRPPVIM VPYLVKKDFP
ITPDYTIPKG SMVCPSTYLA LRDPDVYDKP DEFDPERYYT GDAEEKGAKN YLVFGLGTHY
CLGQLYAQHN LALMIGKASM MLEWAHHPTP QSEEIQVFAC IFPEDHCPLT MKERAL
//
