ID   UPPS_AERPE              Reviewed;         219 AA.
AC   Q9YC66;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=APE_1385;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA80382.1; -; Genomic_DNA.
DR   PIR; H72615; H72615.
DR   AlphaFoldDB; Q9YC66; -.
DR   SMR; Q9YC66; -.
DR   STRING; 272557.APE_1385; -.
DR   EnsemblBacteria; BAA80382; BAA80382; APE_1385.
DR   KEGG; ape:APE_1385; -.
DR   eggNOG; arCOG01532; Archaea.
DR   OMA; GFTQDNT; -.
DR   BRENDA; 2.5.1.29; 171.
DR   BRENDA; 2.5.1.89; 171.
DR   BRENDA; 2.5.1.B35; 171.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1180.10; -; 2.
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; 2.
DR   Pfam; PF01255; Prenyltransf; 2.
DR   SUPFAM; SSF64005; SSF64005; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Reference proteome; Transferase.
FT   CHAIN           1..219
FT                   /note="Tritrans,polycis-undecaprenyl-diphosphate synthase
FT                   (geranylgeranyl-diphosphate specific)"
FT                   /id="PRO_0000123726"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         13..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         59..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         174..176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   219 AA;  25776 MW;  EDF1CCCAEE2D1212 CRC64;
     MGQPRAIGII PDGNRRWASL RGENLYIAYY TGYRNVKRIL TYIRDFYPAI RSVYLYVLSR
     DNCSKRSRAE LSILYRIMRR SIERDIAEIE KGGASLVIVG DINHPNLPDN IRESLAPYHF
     DMYLKKGSLP DGRRVVAGLC YDPFWEIEHY TPKTLPSRLL DEIDLVIRTG GEKRLSSFFP
     LLTRYAELYF IDKLWPDFTR EDLDRAVQWF STRRRPMGR