ID FDFT_USTMA Reviewed; 572 AA.
AC Q92459; Q4P689;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-APR-2013, entry version 95.
DE RecName: Full=Squalene synthase;
DE Short=SQS;
DE Short=SS;
DE EC=2.5.1.21;
DE AltName: Full=FPP:FPP farnesyltransferase;
DE AltName: Full=Farnesyl-diphosphate farnesyltransferase;
GN Name=ERG9; ORFNames=UM04374;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IMI 103761;
RA Corran A.J.;
RT "Squalene synthase in plant pathogenic fungi.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T.,
RA Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U.,
RA Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen
RT Ustilago maydis.";
RL Nature 444:97-101(2006).
CC -!- FUNCTION: Catalyzes the condensation of 2 two farnesyl
CC pyrophosphate moieties to form squalene. It is the first committed
CC enzyme of the sterol biosynthesis pathway. Required for the
CC biosynthesis of ergosterol (By similarity).
CC -!- CATALYTIC ACTIVITY: 2 farnesyl diphosphate + NAD(P)H = squalene +
CC 2 diphosphate + NAD(P)(+).
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol
CC from farnesyl diphosphate: step 1/3.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
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DR EMBL; X99718; CAA68054.1; -; Genomic_DNA.
DR EMBL; AACP01000154; EAK85649.1; -; Genomic_DNA.
DR RefSeq; XP_760521.1; XM_755428.1.
DR ProteinModelPortal; Q92459; -.
DR STRING; 5270.UM04374.1; -.
DR EnsemblFungi; UM04374T0; UM04374P0; UM04374.
DR GeneID; 3632482; -.
DR KEGG; uma:UM04374.1; -.
DR eggNOG; COG1562; -.
DR HOGENOM; HOG000186940; -.
DR KO; K00801; -.
DR OMA; FNFVAIP; -.
DR OrthoDB; EOG4BP4MQ; -.
DR UniPathway; UPA00767; UER00751.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IEA:EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0051996; F:squalene synthase activity; IEA:EC.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR InterPro; IPR006449; Squal_synth.
DR InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR InterPro; IPR008949; Terpenoid_synth.
DR Pfam; PF00494; SQS_PSY; 1.
DR SUPFAM; SSF48576; Terpenoid_synth; 1.
DR TIGRFAMs; TIGR01559; squal_synth; 1.
DR PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 3: Inferred from homology;
KW Complete proteome; Endoplasmic reticulum; Isoprene biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Multifunctional enzyme; NADP; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 572 Squalene synthase.
FT /FTId=PRO_0000067452.
FT TRANSMEM 316 336 Helical; (Potential).
FT TRANSMEM 492 512 Helical; (Potential).
FT CONFLICT 71 72 EL -> DV (in Ref. 1; CAA68054).
FT CONFLICT 428 428 S -> T (in Ref. 1; CAA68054).
SQ SEQUENCE 572 AA; 65523 MW; 26FA62E2CA677C10 CRC64;
MGLLSYILLG FTHPSELRAM IGYKVWRDPL NDIKANPQAS GWDRQRMRDC WGFLDLTSRS
FAAVIKELKG ELSRVICLFY LVLRALDTVE DDMTIPAQRK IPLLVNFYKY LEQPGWNFTE
SGPNEKDRQL LVEFDKVIAE YQLLDVGYKT VISDITAKMG AGMASYIELS AKGPLKVAMW
KHFDLYCHFV AGLVGEGLSR LFSESKLERP WLGHQLELSN HMGLFLQKTN IIRDYAEDCE
EGRYFWPQQC WGDDFAKFES QPDVAKGIIE IKPGHFRPAD NELGQRSMYV LSSMLLDAMS
HATHALDYLA LLKEQSVFNF CAIPQVMAIA TLELMFNNPD VFKKNVKIRK GVAVGLILRA
VNPRDVAYTF LHYSRKMHAR LSPADPNFTR WSVELARIEQ WCETYYPSFI AAASEGKPTD
IRANALRSWS ESRRTQALIL KQAKLNGSDA STLDAKSVLE AAQNSALDPR DLMTEDERAA
QDKRDRDQMV KFFLIILVGM VTFMGIVALI TWEIVWWWTM DTPDPLSVYV KHAYYLVKTQ
GWSTVKEVLR TTRLSFEHVW KHGLTSPPKL EL
//
