AC   MF_01139;
DC   Protein; auto
TR   HAMAP; MF_01139; -; 1; level=0
XX
Names: ISPT
XX
case <OC:Gammaproteobacteria>
ID   UPPS
DE   RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific);
DE            EC=2.5.1.31;
DE   AltName: Full=Ditrans,polycis-undecaprenylcistransferase;
DE   AltName: Full=Undecaprenyl diphosphate synthase;
DE            Short=UDS;
DE   AltName: Full=Undecaprenyl pyrophosphate synthase;
DE            Short=UPP synthase;
GN   Name=uppS;
else case <OC:Archaea>
ID   UPPS
DE   RecName: Full=Tritrans,polycis-undecaprenyl-diphosphate synthase (geranylgeranyl-diphosphate 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;
else
ID   ISPT
DE   RecName: Full=Isoprenyl transferase;
DE            EC=2.5.1.-;
end case
XX
case <OC:Gammaproteobacteria>
CC   -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC       diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield
CC       (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-
CC       trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in
CC       the biosynthesis of bacterial cell wall polysaccharide components such
CC       as peptidoglycan and lipopolysaccharide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-
CC         trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate;
CC         Xref=Rhea:RHEA:27551, ChEBI:CHEBI:33019, ChEBI:CHEBI:58405,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.31;
else case <OC:Archaea>
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.
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;
else
CC   -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC       with allylic pyrophosphates generating different type of terpenoids.
end case
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 magnesium ions per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the UPP synthase family.
XX
DR   Pfam; PF01255; Prenyltransf; 1; trigger=no
DR   NCBIfam; TIGR00055; UppS; 1; trigger=no
DR   PROSITE; PS01066; UPP_SYNTHASE; 1; trigger=no
XX
KW   Magnesium
KW   Metal-binding
KW   Transferase
case <OC:Gammaproteobacteria>
KW   Cell shape
KW   Cell wall biogenesis/degradation
KW   Peptidoglycan synthesis
end case
XX
case <OC:Gammaproteobacteria>
GO   GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity
GO   GO:0009252; P:peptidoglycan biosynthetic process
end case
GO   GO:0000287; F:magnesium ion binding
GO   GO:0004659; F:prenyltransferase activity
XX
FT   From: UPPS_ECOLI (P60472)
FT   ACT_SITE        26
FT   Condition: D
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT   Condition: N
FT   BINDING         27..30
FT                   /ligand="substrate"
FT   Condition: G-N-x-[RK]
FT   BINDING         71..73
FT                   /ligand="substrate"
FT   Condition: S-x-[ED]
FT   BINDING         200..202
FT                   /ligand="substrate"
FT   Condition: R-x-S
FT   BINDING         31
FT                   /ligand="substrate"
FT   Condition: [WF]
FT   BINDING         39
FT                   /ligand="substrate"
FT   Condition: [RK]
FT   BINDING         43
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         75
FT                   /ligand="substrate"
FT   Condition: [WF]
FT   BINDING         77
FT                   /ligand="substrate"
FT   Condition: [RK]
FT   BINDING         194
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         26
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
case <OC:Enterobacterales>
FT   BINDING         199
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: H
end case
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: E
XX
Size: 219-339;
Related: None;
Template: P60472; O82827; Q9HH76; P9WFF7; A0R0S4; P9WFF5; A0R2W4; Q47SS3; Q47RM6;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: <crtB>
 Cter: None
Duplicate: in NOSS1, BRADU, STRAW, STRCO, TROW8, TROWT
Plasmid: in STRCO
Comments: Actinomycetota possess different types of isoprenyl transferases (decaprenyl
 diphosphate synthase; trans,polycis-decaprenyl diphosphate synthase; (2Z,6E)-farnesyl
 diphosphate synthase; trans,polycis-polyprenyl diphosphate synthase) which are all
 homologous to ISPT in primary sequence (and match the family MF_01139) but with a
 different substrate specificity (isoprenyl acceptor) and chain-length determination
 due to a few residues.
XX
# Revision 1.36 2023/06/01
//