ID   HPNC_ZYMMO              Reviewed;         297 AA.
AC   Q5NP67; O34287;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Hydroxysqualene synthase {ECO:0000303|PubMed:26258173};
DE            Short=HSQ synthase {ECO:0000303|PubMed:26258173};
DE            Short=HSQase {ECO:0000303|PubMed:26258173};
DE            EC=4.2.3.156 {ECO:0000269|PubMed:26258173};
GN   Name=hpnC {ECO:0000303|PubMed:9714766};
GN   OrderedLocusNames=ZMO0869 {ECO:0000312|EMBL:AAV89493.1};
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=9714766; DOI=10.1016/s0005-2760(98)00064-2;
RA   Perzl M., Reipen I.G., Schmitz S., Poralla K., Sahm H., Sprenger G.A.,
RA   Kannenberg E.L.;
RT   "Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium
RT   japonicum that function in the biosynthesis of hopanoid lipids.";
RL   Biochim. Biophys. Acta 1393:108-118(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Um H.W.;
RT   "Sequence analysis of 43F4 fosmid clone of Zymomonas mobilis.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=26258173; DOI=10.1021/acscentsci.5b00115;
RA   Pan J.J., Solbiati J.O., Ramamoorthy G., Hillerich B.S., Seidel R.D.,
RA   Cronan J.E., Almo S.C., Poulter C.D.;
RT   "Biosynthesis of squalene from farnesyl diphosphate in bacteria: three
RT   steps catalyzed by three enzymes.";
RL   ACS Cent. Sci. 1:77-82(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of the hopanoid precursor
CC       squalene (SQ) from farnesyl diphosphate (FPP). Catalyzes the second
CC       step, the conversion of presqualene diphosphate (PSPP) to
CC       hydroxysqualene (HSQ). {ECO:0000269|PubMed:26258173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + presqualene diphosphate = diphosphate + hydroxysqualene;
CC         Xref=Rhea:RHEA:47984, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57310, ChEBI:CHEBI:88123; EC=4.2.3.156;
CC         Evidence={ECO:0000269|PubMed:26258173};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; hopanoid biosynthesis.
CC       {ECO:0000269|PubMed:26258173, ECO:0000269|PubMed:9714766}.
CC   -!- SIMILARITY: Belongs to the phytoene/squalene synthase family. HpnC
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ001401; CAA04732.1; -; Genomic_DNA.
DR   EMBL; AF203881; AAF12832.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89493.1; -; Genomic_DNA.
DR   RefSeq; WP_011240735.1; NC_006526.2.
DR   AlphaFoldDB; Q5NP67; -.
DR   SMR; Q5NP67; -.
DR   STRING; 264203.ZMO0869; -.
DR   EnsemblBacteria; AAV89493; AAV89493; ZMO0869.
DR   GeneID; 58026673; -.
DR   KEGG; zmo:ZMO0869; -.
DR   eggNOG; COG1562; Bacteria.
DR   HOGENOM; CLU_037269_0_1_5; -.
DR   OMA; DYCRYSA; -.
DR   OrthoDB; 1449625at2; -.
DR   BRENDA; 4.2.3.156; 6765.
DR   UniPathway; UPA00337; -.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00683; Trans_IPPS_HH; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR017827; HSQ_synthase_HpnC.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR002060; Squ/phyt_synthse.
DR   InterPro; IPR033904; Trans_IPPS_HH.
DR   PANTHER; PTHR31480:SF17; PTHR31480:SF17; 1.
DR   Pfam; PF00494; SQS_PSY; 1.
DR   SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   TIGRFAMs; TIGR03464; HpnC; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..297
FT                   /note="Hydroxysqualene synthase"
FT                   /id="PRO_0000441692"
FT   CONFLICT        1..9
FT                   /note="MEGACASTY -> MWKGRAQARN (in Ref. 1; CAA04732 and 2;
FT                   AAF12832)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="T -> N (in Ref. 1; CAA04732 and 2; AAF12832)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211
FT                   /note="R -> C (in Ref. 1; CAA04732 and 2; AAF12832)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        238..241
FT                   /note="GFSA -> SFSV (in Ref. 1; CAA04732 and 2; AAF12832)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   297 AA;  32970 MW;  108A8EC49E949E8A CRC64;
     MEGACASTYR SVSIKTKNKL NAAALVSGKG HQDENFPVAS FLINPEYRPI IMAFYQFARQ
     ADDVADNVIA SKKDRLAILE DMRSSLTGES QSEPNAVVLR QTLITHGLDH TIVHGLDLLE
     AFRRDVSVNR YENWDALMDY CRYSASPVGR FVLDVHKESR NLWPMNDALC TALQVINHLQ
     DCGKDYRMMN RIYIPSDIME AVGATAGDLG RFHASLPLRQ AIETAALKTK SLLKRSSGFS
     AAIHDKRLGV EVAVIQRLAE SLTECLTKHD PLSERVHHNK AETLGLAFVA AAGRLFS