ACO1_AJECA
ID ACO1_AJECA Reviewed; 476 AA.
AC Q12618;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Acyl-CoA desaturase;
DE EC=1.14.19.1 {ECO:0000305|PubMed:8538376};
DE AltName: Full=Delta(9)-desaturase {ECO:0000305};
DE Short=Delta-9 desaturase {ECO:0000305};
DE AltName: Full=Fatty acid desaturase {ECO:0000305};
DE AltName: Full=Stearoyl-CoA desaturase {ECO:0000305};
GN Name=OLE1 {ECO:0000303|PubMed:8538376};
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 38904 / Downs;
RX PubMed=8538376; DOI=10.1007/bf02537480;
RA Gargano S., Di Lallo G., Kobayashi G.S., Maresca B.;
RT "A temperature-sensitive strain of Histoplasma capsulatum has an altered
RT D9-fatty acid desaturase gene.";
RL Lipids 30:899-906(1995).
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. Has high specificity and catalyzes the
CC insertion of a cis double bond at the delta-9 position into fatty acyl-
CC CoA substrates including palmitoyl-CoA and stearoyl-CoA. Contributes to
CC the biosynthesis of membrane phospholipids, cholesterol esters and
CC triglycerides. {ECO:0000305|PubMed:8538376}.
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:0000305|PubMed:8538376};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P13516};
CC Note=Expected to bind 2 Fe(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:P13516};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The histidine box domains are involved in binding the catalytic
CC metal ions. {ECO:0000250|UniProtKB:O00767}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X85963; CAA59939.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12618; -.
DR SMR; Q12618; -.
DR BioCyc; MetaCyc:MON-17616; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-EC.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR Gene3D; 3.10.120.10; -; 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; PTHR11351; 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; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 1: Evidence at protein level;
KW Electron transport; Fatty acid biosynthesis; Fatty acid metabolism; Heme;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..476
FT /note="Acyl-CoA desaturase"
FT /id="PRO_0000185404"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..80
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..199
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 349..427
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 101..106
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 138..142
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 275..279
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 141
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 275
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 278
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 279
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 384
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:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 410
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:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 476 AA; 53791 MW; A91A9CE2A865CADB CRC64;
MALNEAPTAS PVAETAAGGK DVVTDAARRP NSEPKKVHIT DTPITLANWH KHISWLNVTL
IIAIPIYGLV QAYWVPLHLK TALWAVVYYF MTGLGITAGY HRLWAHCSYS ATLPLKIYLA
AVGGGAVEGS IRWWARGHRA HHRYTDTDKD PYSVRKGLLY SHIGWMVMKQ NPKRIGRTEI
TDLNEDPVVV WQHRNYLKVV IFMGIVFPML VSGLGWGDWF GGFIYAGILR IFFVQQATFC
VNSLAHWLGD QPFDDRNSPR DHIVTALVTL GEGYHNFHHE FPSDYRNAIE WHQYDPTKWT
IWIWKQLGLA YDLKQFRANE IEKGRVQQLQ KKIDQRRAKL DWGIPLEQLP VIEWDDYVDQ
AKNGRGLIAI AGVVHDVTDF IKDHPGGKAM INSGIGKDAT AMFNGGVYNH SNAAHNQLST
MRVGVIRGGC EVEIWKRAQK ENKEVESVRD EYGNRIVRAG AQVTKIPEPI TTADAA
