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Protein

Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)

Gene

ispU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.1 Publication

Catalytic activityi

(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + di-trans,octa-cis-undecaprenyl diphosphate.

Cofactori

Mg2+2 PublicationsNote: Binds 2 magnesium ions per subunit.2 Publications

Enzyme regulationi

Inhibited by bisphosphonates.1 Publication

Kineticsi

  1. KM=0.4 µM for FPP (at pH 7.5 and at 25 degrees Celsius)1 Publication
  2. KM=4.1 µM for IPP (at pH 7.5 and at 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei26 – 261
    Metal bindingi26 – 261Magnesium
    Binding sitei31 – 311Substrate1 Publication
    Binding sitei39 – 391Substrate1 Publication
    Binding sitei43 – 431Substrate1 Publication
    Sitei69 – 691Required for continued chain elongation
    Active sitei74 – 741Proton acceptorBy similarity
    Binding sitei75 – 751Substrate1 Publication
    Binding sitei77 – 771Substrate1 Publication
    Sitei137 – 1371Important for determining product length
    Binding sitei194 – 1941Substrate1 Publication
    Metal bindingi199 – 1991Magnesium
    Metal bindingi213 – 2131Magnesium
    Binding sitei213 – 2131Isopentenyl diphosphate

    GO - Molecular functioni

    • di-trans,poly-cis-decaprenylcistransferase activity Source: EcoCyc
    • magnesium ion binding Source: EcoCyc

    GO - Biological processi

    • cell cycle Source: UniProtKB-KW
    • cell division Source: UniProtKB-KW
    • cell wall organization Source: UniProtKB-KW
    • Gram-negative-bacterium-type cell wall biogenesis Source: EcoCyc
    • peptidoglycan biosynthetic process Source: EcoCyc
    • polyprenol biosynthetic process Source: EcoCyc
    • regulation of cell shape Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:UPPSYN-MONOMER.
    ECOL316407:JW0169-MONOMER.
    MetaCyc:UPPSYN-MONOMER.
    BRENDAi2.5.1.31. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (EC:2.5.1.31)
    Alternative name(s):
    Ditrans,polycis-undecaprenylcistransferase
    Undecaprenyl diphosphate synthase
    Short name:
    UDS
    Undecaprenyl pyrophosphate synthase
    Short name:
    UPP synthase
    Gene namesi
    Name:ispU
    Synonyms:rth, uppS, yaeS
    Ordered Locus Names:b0174, JW0169
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13329. ispU.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoCyc
    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261D → A: Great decrease in activity. 1 Publication
    Mutagenesisi31 – 311W → F: Decrease in activity; reduced affinity for decaprenyl diphosphate substrate analog. 1 Publication
    Mutagenesisi43 – 431H → A: Great decreases in the catalytic efficiency and the affinity for FPP and IPP. 1 Publication
    Mutagenesisi62 – 621I → A: Formation predominantly of C(60) and C(65) polymers rather than the C(55) polymer. 1 Publication
    Mutagenesisi69 – 691A → L: Produces shorter polymers. 1 Publication
    Mutagenesisi71 – 711S → A: Decrease in activity. 1 Publication
    Mutagenesisi73 – 731E → A: Slight decrease in activity. 2 Publications
    Mutagenesisi74 – 741N → A: Decrease in activity. 1 Publication
    Mutagenesisi75 – 751W → A or F: Decrease in activity; reduced affinity for decaprenyl diphosphate substrate analog. 2 Publications
    Mutagenesisi77 – 771R → A: Decrease in activity. 1 Publication
    Mutagenesisi81 – 811E → A: Slight decrease in activity. 1 Publication
    Mutagenesisi91 – 911W → F: Decrease in affinity for IPP. 1 Publication
    Mutagenesisi103 – 1031H → A: No effect. 1 Publication
    Mutagenesisi105 – 1051V → A: Formation predominantly of C(60), C(65) and C(70) polymers rather than the C(55) polymer. 1 Publication
    Mutagenesisi137 – 1371L → A: Formation predominantly of a C(70) polymer rather than the C(55) polymer. 1 Publication
    Mutagenesisi143 – 1431A → V: No effect on polymer length. 1 Publication
    Mutagenesisi149 – 1491W → F: Decrease in affinity for IPP. 1 Publication
    Mutagenesisi150 – 1501D → A: Great decrease in affinity for the substrate. 1 Publication
    Mutagenesisi190 – 1901D → A: No effect. 1 Publication
    Mutagenesisi198 – 1981E → A: No effect. 1 Publication
    Mutagenesisi199 – 1991H → A: Great decreases in the catalytic efficiency and in the affinity for IPP; when associated with A-213. 1 Publication
    Mutagenesisi207 – 2071W → F: Decrease in affinity for both IPP and decaprenyl diphosphate substrate analog. 1 Publication
    Mutagenesisi213 – 2131E → A: Great decrease in activity; reduced affinity for IPP. Great decreases in the catalytic efficiency and in the affinity for IPP; when associated with A-199. 2 Publications
    Mutagenesisi218 – 2181D → A: Slight decrease in activity. 1 Publication
    Mutagenesisi221 – 2211W → F: Decrease in affinity for IPP. 1 Publication
    Mutagenesisi223 – 2231D → A: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 253253Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)PRO_0000123609Add
    BLAST

    Proteomic databases

    PaxDbiP60472.
    PRIDEiP60472.

    Interactioni

    Subunit structurei

    Homodimer.6 Publications

    Protein-protein interaction databases

    BioGridi4260767. 393 interactions.
    DIPiDIP-48251N.
    IntActiP60472. 4 interactions.
    STRINGi511145.b0174.

    Structurei

    Secondary structure

    1
    253
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 173Combined sources
    Beta strandi19 – 257Combined sources
    Helixi28 – 347Combined sources
    Helixi39 – 5921Combined sources
    Beta strandi63 – 686Combined sources
    Helixi72 – 754Combined sources
    Helixi83 – 908Combined sources
    Helixi93 – 10210Combined sources
    Beta strandi106 – 1116Combined sources
    Helixi113 – 1153Combined sources
    Helixi118 – 13114Combined sources
    Beta strandi138 – 1447Combined sources
    Helixi147 – 16418Combined sources
    Helixi169 – 1713Combined sources
    Helixi174 – 1785Combined sources
    Turni182 – 1854Combined sources
    Beta strandi191 – 1977Combined sources
    Beta strandi204 – 2063Combined sources
    Helixi207 – 2093Combined sources
    Beta strandi213 – 2164Combined sources
    Helixi221 – 2233Combined sources
    Helixi226 – 23914Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JP3X-ray1.80A/B1-253[»]
    1UEHX-ray1.73A/B1-253[»]
    1V7UX-ray2.35A/B1-253[»]
    1X06X-ray1.90A1-253[»]
    1X07X-ray2.20A1-253[»]
    1X08X-ray1.90A1-253[»]
    1X09X-ray1.87A1-253[»]
    2E98X-ray1.90A/B1-253[»]
    2E99X-ray2.00A/B1-253[»]
    2E9AX-ray2.10A/B1-253[»]
    2E9CX-ray2.05A/B1-253[»]
    2E9DX-ray2.50A/B1-253[»]
    3QASX-ray1.70A/B1-253[»]
    3SGVX-ray1.61A/B1-253[»]
    3SGXX-ray2.45A/B1-253[»]
    3SH0X-ray1.84A/B1-253[»]
    3TH8X-ray2.11A/B1-253[»]
    3WYJX-ray2.10A/B1-253[»]
    4H2JX-ray1.81A/B1-253[»]
    4H2MX-ray1.78A/B1-253[»]
    4H2OX-ray2.14A/B1-253[»]
    4H38X-ray1.95A/B1-253[»]
    4H3AX-ray1.98A/B1-253[»]
    4H3CX-ray1.93A/B1-253[»]
    5CQBX-ray2.20A/B2-253[»]
    5CQJX-ray2.15A/B1-253[»]
    DisProtiDP00516.
    ProteinModelPortaliP60472.
    SMRiP60472. Positions 17-238.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60472.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 305Substrate binding
    Regioni71 – 733Substrate bindingBy similarity
    Regioni200 – 2023Substrate binding

    Sequence similaritiesi

    Belongs to the UPP synthase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CR3. Bacteria.
    COG0020. LUCA.
    HOGENOMiHOG000006054.
    InParanoidiP60472.
    KOiK00806.
    OMAiWAKLKNK.
    OrthoDBiEOG68H89T.
    PhylomeDBiP60472.

    Family and domain databases

    Gene3Di3.40.1180.10. 1 hit.
    HAMAPiMF_01139. ISPT.
    InterProiIPR001441. UPP_synth-like.
    IPR018520. UPP_synth-like_CS.
    [Graphical view]
    PANTHERiPTHR10291. PTHR10291. 1 hit.
    PfamiPF01255. Prenyltransf. 1 hit.
    [Graphical view]
    SUPFAMiSSF64005. SSF64005. 1 hit.
    TIGRFAMsiTIGR00055. uppS. 1 hit.
    PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P60472-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMLSATQPLS EKLPAHGCRH VAIIMDGNGR WAKKQGKIRA FGHKAGAKSV
    60 70 80 90 100
    RRAVSFAANN GIEALTLYAF SSENWNRPAQ EVSALMELFV WALDSEVKSL
    110 120 130 140 150
    HRHNVRLRII GDTSRFNSRL QERIRKSEAL TAGNTGLTLN IAANYGGRWD
    160 170 180 190 200
    IVQGVRQLAE KVQQGNLQPD QIDEEMLNQH VCMHELAPVD LVIRTGGEHR
    210 220 230 240 250
    ISNFLLWQIA YAELYFTDVL WPDFDEQDFE GALNAFANRE RRFGGTEPGD

    ETA
    Length:253
    Mass (Da):28,444
    Last modified:February 16, 2004 - v1
    Checksum:i73DC9534C14CA7B9
    GO

    Sequence cautioni

    The sequence AAB08603.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U70214 Genomic DNA. Translation: AAB08603.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73285.1.
    AP009048 Genomic DNA. Translation: BAA77849.2.
    PIRiF64741.
    RefSeqiNP_414716.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC73285; AAC73285; b0174.
    BAA77849; BAA77849; BAA77849.
    GeneIDi944874.
    KEGGiecj:JW0169.
    eco:b0174.
    PATRICi32115457. VBIEscCol129921_0180.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U70214 Genomic DNA. Translation: AAB08603.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73285.1.
    AP009048 Genomic DNA. Translation: BAA77849.2.
    PIRiF64741.
    RefSeqiNP_414716.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JP3X-ray1.80A/B1-253[»]
    1UEHX-ray1.73A/B1-253[»]
    1V7UX-ray2.35A/B1-253[»]
    1X06X-ray1.90A1-253[»]
    1X07X-ray2.20A1-253[»]
    1X08X-ray1.90A1-253[»]
    1X09X-ray1.87A1-253[»]
    2E98X-ray1.90A/B1-253[»]
    2E99X-ray2.00A/B1-253[»]
    2E9AX-ray2.10A/B1-253[»]
    2E9CX-ray2.05A/B1-253[»]
    2E9DX-ray2.50A/B1-253[»]
    3QASX-ray1.70A/B1-253[»]
    3SGVX-ray1.61A/B1-253[»]
    3SGXX-ray2.45A/B1-253[»]
    3SH0X-ray1.84A/B1-253[»]
    3TH8X-ray2.11A/B1-253[»]
    3WYJX-ray2.10A/B1-253[»]
    4H2JX-ray1.81A/B1-253[»]
    4H2MX-ray1.78A/B1-253[»]
    4H2OX-ray2.14A/B1-253[»]
    4H38X-ray1.95A/B1-253[»]
    4H3AX-ray1.98A/B1-253[»]
    4H3CX-ray1.93A/B1-253[»]
    5CQBX-ray2.20A/B2-253[»]
    5CQJX-ray2.15A/B1-253[»]
    DisProtiDP00516.
    ProteinModelPortaliP60472.
    SMRiP60472. Positions 17-238.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260767. 393 interactions.
    DIPiDIP-48251N.
    IntActiP60472. 4 interactions.
    STRINGi511145.b0174.

    Proteomic databases

    PaxDbiP60472.
    PRIDEiP60472.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73285; AAC73285; b0174.
    BAA77849; BAA77849; BAA77849.
    GeneIDi944874.
    KEGGiecj:JW0169.
    eco:b0174.
    PATRICi32115457. VBIEscCol129921_0180.

    Organism-specific databases

    EchoBASEiEB3113.
    EcoGeneiEG13329. ispU.

    Phylogenomic databases

    eggNOGiENOG4105CR3. Bacteria.
    COG0020. LUCA.
    HOGENOMiHOG000006054.
    InParanoidiP60472.
    KOiK00806.
    OMAiWAKLKNK.
    OrthoDBiEOG68H89T.
    PhylomeDBiP60472.

    Enzyme and pathway databases

    BioCyciEcoCyc:UPPSYN-MONOMER.
    ECOL316407:JW0169-MONOMER.
    MetaCyc:UPPSYN-MONOMER.
    BRENDAi2.5.1.31. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP60472.
    PROiP60472.

    Family and domain databases

    Gene3Di3.40.1180.10. 1 hit.
    HAMAPiMF_01139. ISPT.
    InterProiIPR001441. UPP_synth-like.
    IPR018520. UPP_synth-like_CS.
    [Graphical view]
    PANTHERiPTHR10291. PTHR10291. 1 hit.
    PfamiPF01255. Prenyltransf. 1 hit.
    [Graphical view]
    SUPFAMiSSF64005. SSF64005. 1 hit.
    TIGRFAMsiTIGR00055. uppS. 1 hit.
    PROSITEiPS01066. UPP_SYNTHASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
      Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene."
      Apfel C.M., Takacs B., Fountoulakis M., Stieger M., Keck W.
      J. Bacteriol. 181:483-492(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesis."
      Kato J., Fujisaki S., Nakajima K., Nishimura Y., Sato M., Nakano A.
      J. Bacteriol. 181:2733-2738(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis."
      Pan J.-J., Yang L.-W., Liang P.-H.
      Biochemistry 39:13856-13861(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-26; GLU-73; ASP-150; ASP-190; GLU-198; GLU-213; ASP-218 AND ASP-223.
    8. "Probing the conformational change of Escherichia coli undecaprenyl pyrophosphate synthase during catalysis using an inhibitor and tryptophan mutants."
      Chen Y.-H., Chen A.P.-C., Chen C.-T., Wang A.H.-J., Liang P.-H.
      J. Biol. Chem. 277:7369-7376(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-31; TRP-75; TRP-91; TRP-149; TRP-207 AND TRP-221.
    9. "Mechanism of cis-prenyltransferase reaction probed by substrate analogues."
      Lu Y.P., Liu H.G., Teng K.H., Liang P.H.
      Biochem. Biophys. Res. Commun. 400:758-762(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REACTION MECHASNISM.
    10. "Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis."
      Ko T.-P., Chen Y.-K., Robinson H., Tsai P.-C., Gao Y.-G., Chen A.P.-C., Wang A.H.-J., Liang P.-H.
      J. Biol. Chem. 276:47474-47482(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-240, MUTAGENESIS OF ILE-62; ALA-69; SER-71; GLU-73; ASN-74; TRP-75; ARG-77; GLU-81; HIS-103; VAL-105; LEU-137 AND ALA-143, SUBUNIT.
    11. "Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton."
      Chang S.-Y., Ko T.-P., Liang P.-H., Wang A.H.-J.
      J. Biol. Chem. 278:29298-29307(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 13-240 IN COMPLEX WITH SUBSTRATES ANALOGS AND MAGNESIUM IONS, FUNCTION AS AN UNDECAPRENYL DIPHOSPHATE SYNTHASE, MUTAGENESIS OF HIS-43; HIS-199 AND GLU-213, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
    12. "Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies."
      Chang S.Y., Ko T.P., Chen A.P., Wang A.H., Liang P.H.
      Protein Sci. 13:971-978(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, COFACTOR, SUBUNIT.
    13. "Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis."
      Guo R.T., Ko T.P., Chen A.P., Kuo C.J., Wang A.H., Liang P.H.
      J. Biol. Chem. 280:20762-20774(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF WILD-TYPE AND OF MUTANT ALA-26 IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, ENZYME REGULATION, SUBUNIT.
    15. "Applying molecular dynamics simulations to identify rarely sampled ligand-bound conformational states of undecaprenyl pyrophosphate synthase, an antibacterial target."
      Sinko W., de Oliveira C., Williams S., Van Wynsberghe A., Durrant J.D., Cao R., Oldfield E., McCammon J.A.
      Chem. Biol. Drug Des. 77:412-420(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiUPPS_ECOLI
    AccessioniPrimary (citable) accession number: P60472
    Secondary accession number(s): P75668, Q47675, Q9R2E4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 16, 2004
    Last sequence update: February 16, 2004
    Last modified: April 13, 2016
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.