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Database: UniProt
Entry: G7XGL3_ASPKW
LinkDB: G7XGL3_ASPKW
Original site: G7XGL3_ASPKW 
ID   G7XGL3_ASPKW            Unreviewed;       456 AA.
AC   G7XGL3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Acyl-CoA desaturase {ECO:0000256|PIRNR:PIRNR000345};
DE            EC=1.14.19.1 {ECO:0000256|PIRNR:PIRNR000345};
GN   ORFNames=AKAW_04186 {ECO:0000313|EMBL:GAA86072.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA86072.1};
RN   [1] {ECO:0000313|EMBL:GAA86072.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA86072.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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}.
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DR   EMBL; DF126455; GAA86072.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XGL3; -.
DR   STRING; 1033177.G7XGL3; -.
DR   VEuPathDB; FungiDB:AKAW_04186; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   eggNOG; KOG1600; Eukaryota.
DR   InParanoid; G7XGL3; -.
DR   Proteomes; UP000006812; 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; STEAROYL-COA DESATURASE-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|ARBA:ARBA00023160,
KW   ECO:0000256|PIRNR:PIRNR000345};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW   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|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR000345};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   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   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        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        64..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          331..409
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
SQ   SEQUENCE   456 AA;  51812 MW;  8536E528F7077D41 CRC64;
     MSAKPADASR PRAADPKKVH IADTVMTRGN WYKHVNWLNV FLIIGIPLYG CVQALWVPLQ
     VKTAIWAVIY YFFTGLGITA GYHRLWAHCS YSARLPLRIW LAAVGGGAVE GSIRWWARDH
     RAHHRYTDTD KDPYSVRKGL LYSHLGWMVM KQNPKRIGRT DISDLNEDPV VVWQHRNYLK
     VVFTMGLIVP MLVSGLGWGD WWGGFVYAGI LRIFFVQQAT FCVNSLAHWL GDQPFDDRNS
     PRDHVITALV TLGEGYHNFH HEFPSDYRNA IEWHQYDPTK WSIWAWKQLG LAYDLKKFRA
     NEIEKGRVQQ LQKKLDQKRS RLDWGTPLDQ LPVMEWDDYV EQAKNGRGLI AIAGVVHDVT
     DFIKDHPGGK AMINSGIGKD ATAMFNGGVY YHSNAAHNLL STMRVGVIRG GCEVEIWKRA
     QKEGAGYVRD DAGQRVIRAG EQVTKIPEPI PTADAA
//
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