ACO1_SCHPO
ID ACO1_SCHPO Reviewed; 479 AA.
AC O94523; Q9UU24;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable acyl-CoA desaturase;
DE EC=1.14.19.1 {ECO:0000250|UniProtKB:P21147};
DE AltName: Full=Delta(9)-desaturase;
DE Short=Delta-9 desaturase;
DE AltName: Full=Fatty acid desaturase;
DE AltName: Full=Stearoyl-CoA desaturase;
GN ORFNames=SPCC1281.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 54-257, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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. Catalyzes the insertion of a cis double bond
CC at the delta-9 position into fatty acyl-CoA substrates including
CC palmitoyl-CoA and stearoyl-CoA. Contributes to the biosynthesis of
CC membrane phospholipids, cholesterol esters and triglycerides.
CC {ECO:0000250|UniProtKB:P21147}.
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:0000250|UniProtKB:P21147};
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:0000269|PubMed:10759889}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:10759889}.
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; CU329672; CAA22827.1; -; Genomic_DNA.
DR EMBL; AB027859; BAA87163.1; -; Genomic_DNA.
DR PIR; T40925; T40925.
DR RefSeq; NP_588170.1; NM_001023159.2.
DR AlphaFoldDB; O94523; -.
DR SMR; O94523; -.
DR BioGRID; 275336; 6.
DR STRING; 4896.SPCC1281.06c.1; -.
DR iPTMnet; O94523; -.
DR MaxQB; O94523; -.
DR PaxDb; O94523; -.
DR PRIDE; O94523; -.
DR EnsemblFungi; SPCC1281.06c.1; SPCC1281.06c.1:pep; SPCC1281.06c.
DR GeneID; 2538753; -.
DR KEGG; spo:SPCC1281.06c; -.
DR PomBase; SPCC1281.06c; -.
DR VEuPathDB; FungiDB:SPCC1281.06c; -.
DR eggNOG; KOG0537; Eukaryota.
DR eggNOG; KOG1600; Eukaryota.
DR HOGENOM; CLU_027359_3_2_1; -.
DR InParanoid; O94523; -.
DR OMA; WNDWRGG; -.
DR PhylomeDB; O94523; -.
DR PRO; PR:O94523; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; ISO:PomBase.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; ISO:PomBase.
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; 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; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00476; FATTY_ACID_DESATUR_1; 1.
PE 3: Inferred from homology;
KW Electron transport; Fatty acid biosynthesis; Fatty acid metabolism; Heme;
KW Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..479
FT /note="Probable acyl-CoA desaturase"
FT /id="PRO_0000185405"
FT TOPO_DOM 1..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..89
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..204
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..229
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 357..433
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 110..115
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 147..151
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 284..288
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 150
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 255
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13516"
FT BINDING 390
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 416
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 CONFLICT 54..59
FT /note="TMQNWW -> GPCKTV (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 54438 MW; ED5666E7B35EFCF2 CRC64;
MTAPSATAFS SATTQPTTEG NASMRKRTIP VVPSVPERKW DPKAPKHIQE QPWTMQNWWR
HLNWLHCMLI FGLPMIAIYG VFTTPLQTKT LIFAIIYYAY SGLGITAGYH RLWSHRAYKA
KKPLEYFLAA GGAAAFEGSI RWWSRDHRAH HRYTDTDKDP YNVKKGFWYA HVGWMIILQN
PRRIGRSDVS DLNSDPFVMF NHRHFLPIAS FMAFIFPSLF CGLLWGDYRG GYFYAGVCRL
VFVHHATFCV NSLAHLIGSQ PFDDTNSARN HFITALVTLG EGNHNYHHAF PNDYRNGLRW
YEYDPTKIFI YIASLFGLAY NLNTFPDNEI QKGIVQQKQK VLDRWRAKLN WGIPLEQLPV
MEFEDFLEQS KTRPLVLING VVHDMTGFEH PGGQGLLRSA FGKDATAAFN GGVYDHTNGA
HNLLSTYRVA VVRGGMEVEV WKSGAGAQLP MKDTQGQKIV RVGEQITRIQ PPIEAAAAN
