ID   UPPS_PICTO              Reviewed;         255 AA.
AC   Q6KZ89;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Tritrans,polycis-undecaprenyl-diphosphate synthase (geranylgeranyl-diphosphate specific) {ECO:0000255|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.89 {ECO:0000255|HAMAP-Rule:MF_01139};
DE   AltName: Full=Undecaprenyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01139};
DE            Short=UDS {ECO:0000255|HAMAP-Rule:MF_01139};
DE   AltName: Full=Undecaprenyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01139};
DE            Short=UPP synthase {ECO:0000255|HAMAP-Rule:MF_01139};
GN   Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; OrderedLocusNames=PTO1378;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC       diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield
CC       (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate
CC       (tritrans,heptacis-UPP). It is probably the precursor of glycosyl
CC       carrier lipids. {ECO:0000255|HAMAP-Rule:MF_01139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7
CC         diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate;
CC         Xref=Rhea:RHEA:27622, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC         ChEBI:CHEBI:60388, ChEBI:CHEBI:128769; EC=2.5.1.89;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01139};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01139};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01139};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01139}.
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DR   EMBL; AE017261; AAT43963.1; -; Genomic_DNA.
DR   RefSeq; WP_011178179.1; NC_005877.1.
DR   AlphaFoldDB; Q6KZ89; -.
DR   SMR; Q6KZ89; -.
DR   STRING; 263820.PTO1378; -.
DR   EnsemblBacteria; AAT43963; AAT43963; PTO1378.
DR   GeneID; 2845319; -.
DR   KEGG; pto:PTO1378; -.
DR   PATRIC; fig|263820.9.peg.1432; -.
DR   eggNOG; arCOG01532; Archaea.
DR   HOGENOM; CLU_038505_2_0_2; -.
DR   OMA; PRTEGHK; -.
DR   OrthoDB; 50844at2157; -.
DR   Proteomes; UP000000438; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 3.40.1180.10; -; 1.
DR   HAMAP; MF_01139; ISPT; 1.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR018520; UPP_synth-like_CS.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   PANTHER; PTHR10291; PTHR10291; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   SUPFAM; SSF64005; SSF64005; 1.
DR   TIGRFAMs; TIGR00055; uppS; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Reference proteome; Transferase.
FT   CHAIN           1..255
FT                   /note="Tritrans,polycis-undecaprenyl-diphosphate synthase
FT                   (geranylgeranyl-diphosphate specific)"
FT                   /id="PRO_0000123735"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        82
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         34
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         35..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         79..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         210..212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   255 AA;  29803 MW;  A467B096D8AF0C75 CRC64;
     MSDIGNFVSR IYESKLLEEI KKHPVPGHLG IITDGNRRYA RSIGISENEG HVKGKEKLEE
     VLNWSMEVGI HMVTVYAFST ENFKRKSDEV NFLFNLINDA FIDLLNDERV YKNGIRVKVI
     GDISKLPDYL KETIKRVEGE TNKFKNFRFN LAIGYGGRQE IIDAIKKIGQ DILNGKIKVD
     NINEEMFRSY LYDKTLPDPD LILRTSGEER ISNFLLWQSA YSELYFADVN WPELRKIDFL
     RAIYSYQNRK RRFGE