ID A0A395MPS8_9HYPO Unreviewed; 475 AA.
AC A0A395MPS8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Acyl-CoA desaturase {ECO:0000256|PIRNR:PIRNR000345};
DE EC=1.14.19.1 {ECO:0000256|PIRNR:PIRNR000345};
GN ORFNames=FIE12Z_5974 {ECO:0000313|EMBL:RFN49767.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN49767.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN49767.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN49767.1,
RC ECO:0000313|Proteomes:UP000265631};
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 -!- FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from
CC reduced cytochrome b5 to introduce the first double bond into saturated
CC fatty acyl-CoA substrates. {ECO:0000256|PIRNR:PIRNR000345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA =
CC (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57394; EC=1.14.19.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000345};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRNR:PIRNR000345};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR000345};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295, ECO:0000256|PIRNR:PIRNR000345}.
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:RFN49767.1}.
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DR EMBL; PXXK01000160; RFN49767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MPS8; -.
DR STRING; 2594813.A0A395MPS8; -.
DR OrthoDB; 637961at2759; -.
DR Proteomes; UP000265631; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR InterPro; IPR009160; Acyl-CoA_deSatase_haem/ster-bd.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR001522; FADS-1_CS.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF31; DESATURASE 1, ISOFORM A-RELATED; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF000345; OLE1; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00075; FACDDSATRASE.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|PIRNR:PIRNR000345};
KW Fatty acid biosynthesis {ECO:0000256|PIRNR:PIRNR000345};
KW Fatty acid metabolism {ECO:0000256|PIRNR:PIRNR000345};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000345};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000345};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000345};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR000345};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000345};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000345};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|PIRNR:PIRNR000345}.
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 348..426
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
SQ SEQUENCE 475 AA; 53423 MW; ABE67411B4ADA52F CRC64;
MATATAAGKN ASPFPDGTKD YVPLRAGGPK KDINKPHISD TPMTWSNWPQ HINWLNTTLV
VFVPLMGFIS AYWVPLQLKT ALWAVFYYVH TGLGITAGYH RMWSHSAYKG TTLLKIYLAA
VGAGAVQGSI RWWSYGHRVH HRYTDTEKDP YSVRKGLMYS HMGWMVLKQN PKKQGRTDIT
DLNEDAVVVW QHKNYIKCVL FMALAFPAIV AGLGWGDWWG GLVYAGILRV CFVQQATFCV
NSLAHWLGDQ PFDDRNSPRD HVITALVTLG EGYHNFHHEF PSDYRNAIEW WQYDPTKWSI
WLWKQLGLAY ELKEFRANEI EKGRVQQLQK KLDQKRATLD WGIPLEQLPV VDWDDFVAQS
KAGKGLVAIA GVIHDVTDFI KDHPGGKALI NSAIGKDATA IFNGGVYLHS NAAHNLLSTM
RVGVLRGGCE VEIWKRAQFE NKDITYMNDS AGQRIIRAGS QVTKMVQPAA SADAA
//
