ID   UPPS_SULAC              Reviewed;         262 AA.
AC   Q9HH76; Q4JAP6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Tritrans,polycis-undecaprenyl-diphosphate synthase (GGDP specific);
DE            EC=2.5.1.89;
DE   AltName: Full=Undecaprenyl diphosphate synthase;
DE            Short=UDS;
DE   AltName: Full=Undecaprenyl pyrophosphate synthase;
DE            Short=UPP synthase;
GN   Name=uppS; Synonyms=cpdS; OrderedLocusNames=Saci_0757;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
RP   CHARACTERIZATION.
RX   PubMed=11114943; DOI=10.1128/jb.183.1.401-404.2001;
RA   Hemmi H., Yamashita S., Shimoyama T., Nakayama T., Nishino T.;
RT   "Cloning, expression, and characterization of cis-polyprenyl diphosphate
RT   synthase from the thermoacidophilic archaeon Sulfolobus acidocaldarius.";
RL   J. Bacteriol. 183:401-404(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Generates tritrans,heptacis-undecaprenyl diphosphate from
CC       isopentenyl pyrophosphate (IPP) and geranylgeranyl diphosphate. It is
CC       probably the precursor of glycosyl carrier lipids.
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:0000269|PubMed:11114943};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR   EMBL; AB048249; BAB12723.1; -; Genomic_DNA.
DR   EMBL; CP000077; AAY80133.1; -; Genomic_DNA.
DR   RefSeq; WP_011277635.1; NC_007181.1.
DR   AlphaFoldDB; Q9HH76; -.
DR   SMR; Q9HH76; -.
DR   STRING; 330779.Saci_0757; -.
DR   EnsemblBacteria; AAY80133; AAY80133; Saci_0757.
DR   GeneID; 3473288; -.
DR   KEGG; sai:Saci_0757; -.
DR   PATRIC; fig|330779.12.peg.726; -.
DR   eggNOG; arCOG01532; Archaea.
DR   HOGENOM; CLU_038505_0_4_2; -.
DR   OMA; PRTEGHK; -.
DR   BioCyc; MetaCyc:MON-15683; -.
DR   BRENDA; 2.5.1.89; 6160.
DR   Proteomes; UP000001018; 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   1: Evidence at protein level;
KW   Magnesium; Metal-binding; Reference proteome; Transferase.
FT   CHAIN           1..262
FT                   /note="Tritrans,polycis-undecaprenyl-diphosphate synthase
FT                   (GGDP specific)"
FT                   /id="PRO_0000123741"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        88
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  30871 MW;  C1D3C384A4E0263C CRC64;
     MAKDVITRAL LRPIYKIYEK ILWSQIKDGP FPFHVGIIPD GNRRWARNNR LPLDQGYYTG
     YVKLRDVLTW ILEIGISTVT VFALSAENCE KRTQQELSMI FKYLKIGLDE LLTSDLVHKY
     QVRVKAIGML DKLPEDLKKL VVDLESTTEK YNKKKLILAI CYGGRQEILD AIRKIMNDYK
     LGIIDSKSID ESTFRKYLYD QELSDIDLLI RSSGEIRISN FLLWHLAYSE LFFVDVYWPD
     FRKIDLWRAI RSFQKRKRNF GA