ID A0A1L9NA77_ASPTC Unreviewed; 446 AA.
AC A0A1L9NA77;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Acyl-CoA desaturase {ECO:0000256|PIRNR:PIRNR000345};
DE EC=1.14.19.1 {ECO:0000256|PIRNR:PIRNR000345};
GN ORFNames=ASPTUDRAFT_27262 {ECO:0000313|EMBL:OJI86190.1};
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI86190.1, ECO:0000313|Proteomes:UP000184304};
RN [1] {ECO:0000313|Proteomes:UP000184304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878187; OJI86190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9NA77; -.
DR STRING; 767770.A0A1L9NA77; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_27262; -.
DR OMA; VIDWTEY; -.
DR Proteomes; UP000184304; 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; 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:UP000184304};
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 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..206
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"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 51101 MW; 7148A31B8365AD3B CRC64;
MGERKMNPKV IDGLHDTQPE KSPTAGQSHQ GGFITTLTSW CNKVRWFNFT MLITIPLIAF
LQVPWVPLHR KTLVLSIIYY VTTAISVTAG YHRLWAHRSY SASPTLKWLL AAFGAGAVQG
SIKFWVREHR AHHRYTDTDQ DPYNVKKGLL HAHILWVITK QPRKNNRVDI SDLQNDRVVV
LQHRYYFLAA FFMGWGFPTL VAGLGWNDWH PSVFFVNQAT FCVNSLAHWI GEQPYDDRRS
SRDHLITALI TMGEGYHNFH HEFPSDYRNG IEWYQPDITK WGIKLCEQLG LAYDLKRFRQ
NEIGKSRLQQ VFKKLNVERE SLDWGPPLSK LPVMEWDEYH DKVTQGHHLV LIGGVVHDVS
KFIHEHPGGE SMMRLALGKD ATTLFNGAVY LHSNAANNIL ATLRVAILRG GCEVEIFKQQ
NNSLDMLAKE TPVHVQDQPK SIAGHS
//
