ID   FDFT_USTMA              Reviewed;         572 AA.
AC   Q92459; A0A0D1BZY0; Q4P689;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 134.
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=UMAG_04374;
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., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., 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., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of 2 two farnesyl pyrophosphate
CC       moieties to form squalene. It is the first committed enzyme of the
CC       sterol biosynthesis pathway. Required for the biosynthesis of
CC       ergosterol (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate
CC         + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate +
CC         NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC       farnesyl diphosphate: step 1/3.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC       {ECO:0000305}.
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DR   EMBL; X99718; CAA68054.1; -; Genomic_DNA.
DR   EMBL; CM003153; KIS67272.1; -; Genomic_DNA.
DR   RefSeq; XP_011391077.1; XM_011392775.1.
DR   AlphaFoldDB; Q92459; -.
DR   SMR; Q92459; -.
DR   STRING; 5270.UM04374P0; -.
DR   EnsemblFungi; KIS67272; KIS67272; UMAG_04374.
DR   GeneID; 23564576; -.
DR   KEGG; uma:UMAG_04374; -.
DR   VEuPathDB; FungiDB:UMAG_04374; -.
DR   eggNOG; KOG1459; Eukaryota.
DR   HOGENOM; CLU_031981_2_2_1; -.
DR   InParanoid; Q92459; -.
DR   OMA; RDPLNDI; -.
DR   OrthoDB; 563702at2759; -.
DR   UniPathway; UPA00767; UER00751.
DR   Proteomes; UP000000561; Chromosome 14.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IBA:GO_Central.
DR   GO; GO:0051996; F:squalene synthase activity; IBA:GO_Central.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0045338; P:farnesyl diphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00683; Trans_IPPS_HH; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR002060; Squ/phyt_synthse.
DR   InterPro; IPR006449; Squal_synth-like.
DR   InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR   InterPro; IPR044844; Trans_IPPS_euk-type.
DR   InterPro; IPR033904; Trans_IPPS_HH.
DR   PANTHER; PTHR11626; PTHR11626; 1.
DR   Pfam; PF00494; SQS_PSY; 1.
DR   SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 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   Endoplasmic reticulum; Isoprene biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Membrane; Multifunctional enzyme; NADP;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..572
FT                   /note="Squalene synthase"
FT                   /id="PRO_0000067452"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        492..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        71..72
FT                   /note="EL -> DV (in Ref. 1; CAA68054)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        428
FT                   /note="S -> T (in Ref. 1; CAA68054)"
FT                   /evidence="ECO:0000305"
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