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Database: UniProt
Entry: E4UU46_ARTGP
LinkDB: E4UU46_ARTGP
Original site: E4UU46_ARTGP 
ID   E4UU46_ARTGP            Unreviewed;       436 AA.
AC   E4UU46;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Acyl-CoA desaturase {ECO:0000256|PIRNR:PIRNR000345};
DE            EC=1.14.19.1 {ECO:0000256|PIRNR:PIRNR000345};
GN   ORFNames=MGYG_03817 {ECO:0000313|EMBL:EFR00813.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS989824; EFR00813.1; -; Genomic_DNA.
DR   RefSeq; XP_003173643.1; XM_003173595.1.
DR   AlphaFoldDB; E4UU46; -.
DR   STRING; 535722.E4UU46; -.
DR   GeneID; 10028926; -.
DR   VEuPathDB; FungiDB:MGYG_03817; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   eggNOG; KOG1600; Eukaryota.
DR   HOGENOM; CLU_027359_3_2_1; -.
DR   InParanoid; E4UU46; -.
DR   OMA; WWSSKHR; -.
DR   OrthoDB; 637961at2759; -.
DR   Proteomes; UP000002669; 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   Reference proteome {ECO:0000313|Proteomes:UP000002669};
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        40..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          337..417
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   436 AA;  49375 MW;  DC3E917F7FF6E52E CRC64;
     MAEPAITVSG TDGRKSKSVH DEKKPHITET PMTWQNWHQF VNWLSVCFII IVPLVGLVAA
     YFLPLKRATA IFAVIYYFNT GLGITAGYHR LWAHSSYEAS TPLKIYLAAV GVGAIQGSIR
     WWSSGHRAHH RYTDTKKDPY SVRKGLLYSH IGWMVMKQNP KNIGRSDITD LNQDPIVMWQ
     HRHYIKAVLF MGLVFPTLIC GFGWGDWAGG FVYAGILRAA FVQQATFCVN SLAHWLGEQP
     FDDRHSPRDH VVTALLTLGE GYHNFHHEFP SDYRNAIRWW QYDPTKWAIW TWKQLGLAYN
     LKEFKQNEIE KGLVQQLQKK VDIKRSQLDW GTPISQLPAM IWDDFKTEAA KKNGRALVVI
     AGVIHDVASF IEEHPGGKVL ISSAVGKDAT ALFNGGVYQH SNAAHNLLST MRVGVIYGGG
     EVEIWKRAYS EKTKTI
//
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