UPPS_PYRAB
ID UPPS_PYRAB Reviewed; 264 AA.
AC Q9V157; G8ZJ37;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=PYRAB05720;
GN ORFNames=PAB0394;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49494.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69964.1; -; Genomic_DNA.
DR PIR; G75176; G75176.
DR RefSeq; WP_010867696.1; NC_000868.1.
DR AlphaFoldDB; Q9V157; -.
DR SMR; Q9V157; -.
DR STRING; 272844.PAB0394; -.
DR EnsemblBacteria; CAB49494; CAB49494; PAB0394.
DR GeneID; 1495477; -.
DR KEGG; pab:PAB0394; -.
DR PATRIC; fig|272844.11.peg.610; -.
DR eggNOG; arCOG01532; Archaea.
DR HOGENOM; CLU_038505_2_0_2; -.
DR OMA; PRTEGHK; -.
DR OrthoDB; 50844at2157; -.
DR PhylomeDB; Q9V157; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; Transferase.
FT CHAIN 1..264
FT /note="Tritrans,polycis-undecaprenyl-diphosphate synthase
FT (geranylgeranyl-diphosphate specific)"
FT /id="PRO_0000123736"
FT ACT_SITE 43
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 44..47
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 88..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 219..221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ SEQUENCE 264 AA; 31463 MW; A67D92206D9FA1D9 CRC64;
MIYGILSHVP KIFFKPAYDL YERYLLEKVK AGVLPKHVAI IMDGNRRWAK KREKPPWYGH
LFGSKKLEEI LEWCHELGIR ILTVYAFSTE NFKRSKEEVE RLMQLFEQKF RELVTDKRVH
EYGVRVNVIG RKELLPKSVR DAAEEAERAT RKYNNYVLNV AIAYGGRSEI VDAVKDIVRD
VMDGKLRVED IDEELLKKYL YVPNMPDPDI VIRTGGEVRI SNFLLYQIAY SELFFVDVYF
PEFRKIDFLR IIREFQKRER RFGR
