UPPS_ECOLI
ID UPPS_ECOLI Reviewed; 253 AA.
AC P60472; P75668; Q47675; Q9R2E4;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 152.
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=ispU; Synonyms=rth, uppS, yaeS; OrderedLocusNames=b0174, JW0169;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9882662; DOI=10.1128/jb.181.2.483-492.1999;
RA Apfel C.M., Takacs B., Fountoulakis M., Stieger M., Keck W.;
RT "Use of genomics to identify bacterial undecaprenyl pyrophosphate
RT synthetase: cloning, expression, and characterization of the essential uppS
RT gene.";
RL J. Bacteriol. 181:483-492(1999).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10217761; DOI=10.1128/jb.181.9.2733-2738.1999;
RA Kato J., Fujisaki S., Nakajima K., Nishimura Y., Sato M., Nakano A.;
RT "The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol
RT synthesis, is essential for carrier lipid formation in bacterial cell wall
RT synthesis.";
RL J. Bacteriol. 181:2733-2738(1999).
RN [7]
RP MUTAGENESIS OF ASP-26; GLU-73; ASP-150; ASP-190; GLU-198; GLU-213; ASP-218
RP AND ASP-223.
RX PubMed=11076526; DOI=10.1021/bi001226h;
RA Pan J.-J., Yang L.-W., Liang P.-H.;
RT "Effect of site-directed mutagenesis of the conserved aspartate and
RT glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis.";
RL Biochemistry 39:13856-13861(2000).
RN [8]
RP MUTAGENESIS OF TRP-31; TRP-75; TRP-91; TRP-149; TRP-207 AND TRP-221.
RX PubMed=11744728; DOI=10.1074/jbc.m110014200;
RA Chen Y.-H., Chen A.P.-C., Chen C.-T., Wang A.H.-J., Liang P.-H.;
RT "Probing the conformational change of Escherichia coli undecaprenyl
RT pyrophosphate synthase during catalysis using an inhibitor and tryptophan
RT mutants.";
RL J. Biol. Chem. 277:7369-7376(2002).
RN [9]
RP REACTION MECHANISM.
RX PubMed=20828539; DOI=10.1016/j.bbrc.2010.09.001;
RA Lu Y.P., Liu H.G., Teng K.H., Liang P.H.;
RT "Mechanism of cis-prenyltransferase reaction probed by substrate
RT analogues.";
RL Biochem. Biophys. Res. Commun. 400:758-762(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-240, MUTAGENESIS OF ILE-62;
RP ALA-69; SER-71; GLU-73; ASN-74; TRP-75; ARG-77; GLU-81; HIS-103; VAL-105;
RP LEU-137 AND ALA-143, AND SUBUNIT.
RX PubMed=11581264; DOI=10.1074/jbc.m106747200;
RA Ko T.-P., Chen Y.-K., Robinson H., Tsai P.-C., Gao Y.-G., Chen A.P.-C.,
RA Wang A.H.-J., Liang P.-H.;
RT "Mechanism of product chain length determination and the role of a flexible
RT loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis.";
RL J. Biol. Chem. 276:47474-47482(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 13-240 IN COMPLEX WITH SUBSTRATES
RP ANALOGS AND MAGNESIUM IONS, FUNCTION AS AN UNDECAPRENYL DIPHOSPHATE
RP SYNTHASE, MUTAGENESIS OF HIS-43; HIS-199 AND GLU-213, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=12756244; DOI=10.1074/jbc.m302687200;
RA Chang S.-Y., Ko T.-P., Liang P.-H., Wang A.H.-J.;
RT "Catalytic mechanism revealed by the crystal structure of undecaprenyl
RT pyrophosphate synthase in complex with sulfate, magnesium, and triton.";
RL J. Biol. Chem. 278:29298-29307(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, COFACTOR,
RP AND SUBUNIT.
RX PubMed=15044730; DOI=10.1110/ps.03519904;
RA Chang S.Y., Ko T.P., Chen A.P., Wang A.H., Liang P.H.;
RT "Substrate binding mode and reaction mechanism of undecaprenyl
RT pyrophosphate synthase deduced from crystallographic studies.";
RL Protein Sci. 13:971-978(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF WILD-TYPE AND OF MUTANT ALA-26 IN
RP COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS.
RX PubMed=15788389; DOI=10.1074/jbc.m502121200;
RA Guo R.T., Ko T.P., Chen A.P., Kuo C.J., Wang A.H., Liang P.H.;
RT "Crystal structures of undecaprenyl pyrophosphate synthase in complex with
RT magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles
RT of the metal ion and conserved residues in catalysis.";
RL J. Biol. Chem. 280:20762-20774(2005).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=17535895; DOI=10.1073/pnas.0702254104;
RA Guo R.-T., Cao R., Liang P.-H., Ko T.-P., Chang T.-H., Hudock M.P.,
RA Jeng W.-Y., Chen C.K.-M., Zhang Y., Song Y., Kuo C.-J., Yin F.,
RA Oldfield E., Wang A.H.-J.;
RT "Bisphosphonates target multiple sites in both cis- and trans-
RT prenyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10022-10027(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBUNIT.
RX PubMed=21294851; DOI=10.1111/j.1747-0285.2011.01101.x;
RA Sinko W., de Oliveira C., Williams S., Van Wynsberghe A., Durrant J.D.,
RA Cao R., Oldfield E., McCammon J.A.;
RT "Applying molecular dynamics simulations to identify rarely sampled ligand-
RT bound conformational states of undecaprenyl pyrophosphate synthase, an
RT antibacterial target.";
RL Chem. Biol. Drug Des. 77:412-420(2011).
CC -!- FUNCTION: Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP)
CC from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP).
CC UPP is the precursor of glycosyl carrier lipid in the biosynthesis of
CC bacterial cell wall polysaccharide components such as peptidoglycan and
CC lipopolysaccharide. {ECO:0000269|PubMed:12756244}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12756244, ECO:0000269|PubMed:15044730};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:12756244,
CC ECO:0000269|PubMed:15044730};
CC -!- ACTIVITY REGULATION: Inhibited by bisphosphonates.
CC {ECO:0000269|PubMed:17535895}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 uM for FPP (at pH 7.5 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:12756244};
CC KM=4.1 uM for IPP (at pH 7.5 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:12756244};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11581264,
CC ECO:0000269|PubMed:12756244, ECO:0000269|PubMed:15044730,
CC ECO:0000269|PubMed:15788389, ECO:0000269|PubMed:17535895,
CC ECO:0000269|PubMed:21294851}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB08603.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U70214; AAB08603.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73285.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77849.2; -; Genomic_DNA.
DR PIR; F64741; F64741.
DR RefSeq; NP_414716.1; NC_000913.3.
DR PDB; 1JP3; X-ray; 1.80 A; A/B=1-253.
DR PDB; 1UEH; X-ray; 1.73 A; A/B=1-253.
DR PDB; 1V7U; X-ray; 2.35 A; A/B=1-253.
DR PDB; 1X06; X-ray; 1.90 A; A=1-253.
DR PDB; 1X07; X-ray; 2.20 A; A=1-253.
DR PDB; 1X08; X-ray; 1.90 A; A=1-253.
DR PDB; 1X09; X-ray; 1.87 A; A=1-253.
DR PDB; 2E98; X-ray; 1.90 A; A/B=1-253.
DR PDB; 2E99; X-ray; 2.00 A; A/B=1-253.
DR PDB; 2E9A; X-ray; 2.10 A; A/B=1-253.
DR PDB; 2E9C; X-ray; 2.05 A; A/B=1-253.
DR PDB; 2E9D; X-ray; 2.50 A; A/B=1-253.
DR PDB; 3QAS; X-ray; 1.70 A; A/B=1-253.
DR PDB; 3SGV; X-ray; 1.61 A; A/B=1-253.
DR PDB; 3SGX; X-ray; 2.45 A; A/B=1-253.
DR PDB; 3SH0; X-ray; 1.84 A; A/B=1-253.
DR PDB; 3TH8; X-ray; 2.11 A; A/B=1-253.
DR PDB; 3WYJ; X-ray; 2.10 A; A/B=1-253.
DR PDB; 4H2J; X-ray; 1.81 A; A/B=1-253.
DR PDB; 4H2M; X-ray; 1.78 A; A/B=1-253.
DR PDB; 4H2O; X-ray; 2.14 A; A/B=1-253.
DR PDB; 4H38; X-ray; 1.95 A; A/B=1-253.
DR PDB; 4H3A; X-ray; 1.98 A; A/B=1-253.
DR PDB; 4H3C; X-ray; 1.93 A; A/B=1-253.
DR PDB; 5CQB; X-ray; 2.20 A; A/B=2-253.
DR PDB; 5CQJ; X-ray; 2.15 A; A/B=1-253.
DR PDB; 5ZHE; X-ray; 2.18 A; A/B=1-253.
DR PDBsum; 1JP3; -.
DR PDBsum; 1UEH; -.
DR PDBsum; 1V7U; -.
DR PDBsum; 1X06; -.
DR PDBsum; 1X07; -.
DR PDBsum; 1X08; -.
DR PDBsum; 1X09; -.
DR PDBsum; 2E98; -.
DR PDBsum; 2E99; -.
DR PDBsum; 2E9A; -.
DR PDBsum; 2E9C; -.
DR PDBsum; 2E9D; -.
DR PDBsum; 3QAS; -.
DR PDBsum; 3SGV; -.
DR PDBsum; 3SGX; -.
DR PDBsum; 3SH0; -.
DR PDBsum; 3TH8; -.
DR PDBsum; 3WYJ; -.
DR PDBsum; 4H2J; -.
DR PDBsum; 4H2M; -.
DR PDBsum; 4H2O; -.
DR PDBsum; 4H38; -.
DR PDBsum; 4H3A; -.
DR PDBsum; 4H3C; -.
DR PDBsum; 5CQB; -.
DR PDBsum; 5CQJ; -.
DR PDBsum; 5ZHE; -.
DR AlphaFoldDB; P60472; -.
DR SMR; P60472; -.
DR BioGRID; 4260767; 417.
DR DIP; DIP-48251N; -.
DR IntAct; P60472; 4.
DR STRING; 511145.b0174; -.
DR BindingDB; P60472; -.
DR ChEMBL; CHEMBL4295580; -.
DR DrugBank; DB07409; (1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID.
DR DrugBank; DB07426; [1-HYDROXY-2-(1,1':3',1''-TERPHENYL-3-YLOXY)ETHANE-1,1-DIYL]BIS(PHOSPHONIC ACID).
DR DrugBank; DB07410; [2-(3-DIBENZOFURAN-4-YL-PHENYL)-1-HYDROXY-1-PHOSPHONO-ETHYL]-PHOSPHONIC ACID.
DR DrugBank; DB07404; BPH-608.
DR DrugBank; DB07780; Farnesyl diphosphate.
DR DrugBank; DB04695; Farnesyl thiopyrophosphate.
DR DrugBank; DB04714; ISOPENTENYL PYROPHOSPHATE.
DR SwissLipids; SLP:000001809; -.
DR jPOST; P60472; -.
DR PaxDb; P60472; -.
DR PRIDE; P60472; -.
DR EnsemblBacteria; AAC73285; AAC73285; b0174.
DR EnsemblBacteria; BAA77849; BAA77849; BAA77849.
DR GeneID; 944874; -.
DR KEGG; ecj:JW0169; -.
DR KEGG; eco:b0174; -.
DR PATRIC; fig|511145.12.peg.180; -.
DR EchoBASE; EB3113; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_1_6; -.
DR InParanoid; P60472; -.
DR OMA; PRTEGHK; -.
DR PhylomeDB; P60472; -.
DR BioCyc; EcoCyc:UPPSYN-MON; -.
DR BioCyc; MetaCyc:UPPSYN-MON; -.
DR BRENDA; 2.5.1.31; 2026.
DR SABIO-RK; P60472; -.
DR EvolutionaryTrace; P60472; -.
DR PRO; PR:P60472; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0043164; P:Gram-negative-bacterium-type cell wall biogenesis; IMP:EcoCyc.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IMP:EcoCyc.
DR GO; GO:0016094; P:polyprenol biosynthetic process; IDA:EcoCyc.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd00475; Cis_IPPS; 1.
DR DisProt; DP00516; -.
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 3D-structure; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Magnesium; Metal-binding;
KW Peptidoglycan synthesis; Reference proteome; Transferase.
FT CHAIN 1..253
FT /note="Ditrans,polycis-undecaprenyl-diphosphate synthase
FT ((2E,6E)-farnesyl-diphosphate specific)"
FT /id="PRO_0000123609"
FT ACT_SITE 26
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 26..30
FT /ligand="substrate"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15044730"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15044730"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15044730"
FT BINDING 71..73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15044730"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15044730"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15044730"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 200..202
FT /ligand="substrate"
FT BINDING 213
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT SITE 69
FT /note="Required for continued chain elongation"
FT SITE 137
FT /note="Important for determining product length"
FT MUTAGEN 26
FT /note="D->A: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:11076526"
FT MUTAGEN 31
FT /note="W->F: Decrease in activity; reduced affinity for
FT decaprenyl diphosphate substrate analog."
FT /evidence="ECO:0000269|PubMed:11744728"
FT MUTAGEN 43
FT /note="H->A: Great decreases in the catalytic efficiency
FT and the affinity for FPP and IPP."
FT /evidence="ECO:0000269|PubMed:12756244"
FT MUTAGEN 62
FT /note="I->A: Formation predominantly of C(60) and C(65)
FT polymers rather than the C(55) polymer."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 69
FT /note="A->L: Produces shorter polymers."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 71
FT /note="S->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 73
FT /note="E->A: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:11076526,
FT ECO:0000269|PubMed:11581264"
FT MUTAGEN 74
FT /note="N->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 75
FT /note="W->A,F: Decrease in activity; reduced affinity for
FT decaprenyl diphosphate substrate analog."
FT /evidence="ECO:0000269|PubMed:11581264,
FT ECO:0000269|PubMed:11744728"
FT MUTAGEN 77
FT /note="R->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 81
FT /note="E->A: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 91
FT /note="W->F: Decrease in affinity for IPP."
FT /evidence="ECO:0000269|PubMed:11744728"
FT MUTAGEN 103
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 105
FT /note="V->A: Formation predominantly of C(60), C(65) and
FT C(70) polymers rather than the C(55) polymer."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 137
FT /note="L->A: Formation predominantly of a C(70) polymer
FT rather than the C(55) polymer."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 143
FT /note="A->V: No effect on polymer length."
FT /evidence="ECO:0000269|PubMed:11581264"
FT MUTAGEN 149
FT /note="W->F: Decrease in affinity for IPP."
FT /evidence="ECO:0000269|PubMed:11744728"
FT MUTAGEN 150
FT /note="D->A: Great decrease in affinity for the substrate."
FT /evidence="ECO:0000269|PubMed:11076526"
FT MUTAGEN 190
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:11076526"
FT MUTAGEN 198
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:11076526"
FT MUTAGEN 199
FT /note="H->A: Great decreases in the catalytic efficiency
FT and in the affinity for IPP; when associated with A-213."
FT /evidence="ECO:0000269|PubMed:12756244"
FT MUTAGEN 207
FT /note="W->F: Decrease in affinity for both IPP and
FT decaprenyl diphosphate substrate analog."
FT /evidence="ECO:0000269|PubMed:11744728"
FT MUTAGEN 213
FT /note="E->A: Great decrease in activity; reduced affinity
FT for IPP. Great decreases in the catalytic efficiency and in
FT the affinity for IPP; when associated with A-199."
FT /evidence="ECO:0000269|PubMed:11076526,
FT ECO:0000269|PubMed:12756244"
FT MUTAGEN 218
FT /note="D->A: Slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:11076526"
FT MUTAGEN 221
FT /note="W->F: Decrease in affinity for IPP."
FT /evidence="ECO:0000269|PubMed:11744728"
FT MUTAGEN 223
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:11076526"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1X09"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 39..59
FT /evidence="ECO:0007829|PDB:3SGV"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:3SGV"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:3SGV"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:3SGV"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3SGV"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:3SGV"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3WYJ"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3SGV"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:3SGV"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:3SGV"
SQ SEQUENCE 253 AA; 28444 MW; 73DC9534C14CA7B9 CRC64;
MMLSATQPLS EKLPAHGCRH VAIIMDGNGR WAKKQGKIRA FGHKAGAKSV RRAVSFAANN
GIEALTLYAF SSENWNRPAQ EVSALMELFV WALDSEVKSL HRHNVRLRII GDTSRFNSRL
QERIRKSEAL TAGNTGLTLN IAANYGGRWD IVQGVRQLAE KVQQGNLQPD QIDEEMLNQH
VCMHELAPVD LVIRTGGEHR ISNFLLWQIA YAELYFTDVL WPDFDEQDFE GALNAFANRE
RRFGGTEPGD ETA
