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Database: UniProt
Entry: Q92459
LinkDB: Q92459
Original site: Q92459 
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   14-MAY-2014, entry version 99.
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; TDIAREM; -.
DR   OrthoDB; EOG7GJ6P5; -.
DR   UniPathway; UPA00767; UER00751.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051996; F:squalene synthase activity; IEA:UniProtKB-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; SSF48576; 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
//
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