ID   UPPS_PYRAE              Reviewed;         238 AA.
AC   Q8ZU54;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=PAE2942;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64554.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZU54; -.
DR   SMR; Q8ZU54; -.
DR   STRING; 178306.PAE2942; -.
DR   EnsemblBacteria; AAL64554; AAL64554; PAE2942.
DR   KEGG; pai:PAE2942; -.
DR   PATRIC; fig|178306.9.peg.2203; -.
DR   eggNOG; arCOG01532; Archaea.
DR   HOGENOM; CLU_038505_2_0_2; -.
DR   InParanoid; Q8ZU54; -.
DR   OMA; PRTEGHK; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
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..238
FT                   /note="Tritrans,polycis-undecaprenyl-diphosphate synthase
FT                   (geranylgeranyl-diphosphate specific)"
FT                   /id="PRO_0000123737"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         19..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         64..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         193..195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         206
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   238 AA;  27999 MW;  6C3A087E85CF0EF7 CRC64;
     MWASGSVKIP THIAVIPDGN RRYAKKTGID FYHAYKKGVE KVRNFLTWAL EFRDIKNVTF
     FALSTENLQR SKIELEILFR IFEDELRRTL EDPLIHDNKV RVRFIGDRSL LPGKVVKYID
     ELESVTKNYS NYHLTIALGY GGRAEIVRCI KRVLSGEVRL ETFSEEELFQ CLDTRGIPNP
     EPDVVVRTGG EKRLSNFLLY QTAYSELIFL EKLWPEVERE DLVYIIEEYS RRQRRFGR