ID   HPND_ZYMMO              Reviewed;         291 AA.
AC   H2VFR7; O34288; Q5NP66;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Presqualene diphosphate synthase {ECO:0000303|PubMed:26258173};
DE            Short=PSPP synthase {ECO:0000303|PubMed:26258173};
DE            Short=PSPPase {ECO:0000303|PubMed:26258173};
DE            EC=2.5.1.103 {ECO:0000269|PubMed:26258173};
GN   Name=hpnD {ECO:0000303|PubMed:9714766};
GN   OrderedLocusNames=ZMO0870 {ECO:0000312|EMBL:AAV89494.1};
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 first
CC       step, the formation of presqualene diphosphate (PSPP) from two
CC       molecules of FPP. {ECO:0000269|PubMed:26258173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene
CC         diphosphate; Xref=Rhea:RHEA:22672, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57310, ChEBI:CHEBI:175763; EC=2.5.1.103;
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. HpnD
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ001401; CAA04733.1; -; Genomic_DNA.
DR   EMBL; AF203881; AAF12831.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89494.1; -; Genomic_DNA.
DR   RefSeq; WP_011240736.1; NZ_CP035711.1.
DR   AlphaFoldDB; H2VFR7; -.
DR   SMR; H2VFR7; -.
DR   STRING; 264203.ZMO0870; -.
DR   EnsemblBacteria; AAV89494; AAV89494; ZMO0870.
DR   GeneID; 58026674; -.
DR   KEGG; zmo:ZMO0870; -.
DR   eggNOG; COG1562; Bacteria.
DR   HOGENOM; CLU_037269_1_1_5; -.
DR   OMA; VKAPRIM; -.
DR   OrthoDB; 1449625at2; -.
DR   UniPathway; UPA00337; -.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR   GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00683; Trans_IPPS_HH; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR017828; SQ_synth_HpnD-like.
DR   InterPro; IPR002060; Squ/phyt_synthse.
DR   InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR   InterPro; IPR044843; Trans_IPPS_bact-type.
DR   InterPro; IPR033904; Trans_IPPS_HH.
DR   Pfam; PF00494; SQS_PSY; 1.
DR   SFLD; SFLDG01212; Phytoene_synthase_like; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   TIGRFAMs; TIGR03465; HpnD; 1.
DR   PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
DR   PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..291
FT                   /note="Presqualene diphosphate synthase"
FT                   /id="PRO_0000441694"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32577 MW;  E6E2B062EF31AEA0 CRC64;
     MTSAMKKIQP EAFSEKSSDS QASVSGAKSS SFYIGMRVLP PAEREAMYAI YNFCRQVDDI
     ADDLEGSQEE RKQALDAWRH DINALYAGEP CGQAAFLKEP VARFHLRQED FIAVIDGMAM
     DLKGPIVFPD EATLDLYCDR VASAVGRLSV YVFGMDPNIG ESLAYHLGRA LQLTNILRDI
     DEDAEIGRCY LPREPLEKAG IPLDIEKALA DPRLDKVCRD LAWQAEGHYA ASDHIIHNRP
     KGYLIAPRLM AAAYSALLRK MLAQGWKNPR KKVKHNKLAL LWTLLRLKVT S