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O82827

- UPPS_MICLU

UniProt

O82827 - UPPS_MICLU

Protein

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

Gene

uppS

Organism
Micrococcus luteus (Micrococcus lysodeikticus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate. UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.2 Publications

    Catalytic activityi

    (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + di-trans,octa-cis-undecaprenyl diphosphate.1 Publication

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei29 – 291
    Metal bindingi29 – 291MagnesiumBy similarity
    Binding sitei34 – 341SubstrateBy similarity
    Binding sitei42 – 421Substrate
    Binding sitei46 – 461SubstrateBy similarity
    Active sitei77 – 771Proton acceptorBy similarity
    Binding sitei78 – 781SubstrateBy similarity
    Binding sitei80 – 801SubstrateBy similarity
    Binding sitei197 – 1971SubstrateBy similarity
    Metal bindingi216 – 2161MagnesiumBy similarity

    GO - Molecular functioni

    1. di-trans,poly-cis-decaprenylcistransferase activity Source: UniProtKB-EC
    2. magnesium ion binding Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Magnesium, Metal-binding

    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:uppS
    OrganismiMicrococcus luteus (Micrococcus lysodeikticus)
    Taxonomic identifieri1270 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeMicrococcus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291D → A: Great decrease in activity. 1 Publication
    Mutagenesisi32 – 321G → R: Great decrease in activity. Decrease in activity; when associated with G-42. 1 Publication
    Mutagenesisi33 – 331R → A: Decrease in affinity for decaprenyl diphosphate substrate analog. 1 Publication
    Mutagenesisi42 – 421R → G: Great decrease in activity. Decrease in activity; when associated with R-32. 1 Publication
    Mutagenesisi73 – 731F → A: Decrease in activity; reduced affinity for substrate. 1 Publication
    Mutagenesisi74 – 741S → A: Decrease in activity; reduced affinity for substrate. 1 Publication
    Mutagenesisi76 – 761E → Q: Slight decrease in activity. 1 Publication
    Mutagenesisi77 – 771N → A, D or Q: Great decrease in activity. 1 Publication
    Mutagenesisi78 – 781W → I, R or D: Decrease in activity. 1 Publication
    Mutagenesisi80 – 801R → A: Great decrease in activity. 1 Publication
    Mutagenesisi84 – 841E → Q: Slight decrease in activity. 1 Publication
    Mutagenesisi193 – 1931E → Q: Decrease in activity. 1 Publication
    Mutagenesisi197 – 1971R → S: Great decrease in activity; reduced affinity for substrate. 1 Publication
    Mutagenesisi201 – 2011E → Q: Slight decrease in activity. 1 Publication
    Mutagenesisi203 – 2031R → S: Great decrease in activity; reduced affinity for substrate. 1 Publication
    Mutagenesisi216 – 2161E → Q: Great decrease in activity; reduced affinity for substrate. 1 Publication
    Mutagenesisi221 – 2211D → A: Decrease in activity. 1 Publication
    Mutagenesisi226 – 2261D → A: Slight decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 249249Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)PRO_0000123637Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    249
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 287
    Helixi31 – 377
    Helixi42 – 6322
    Beta strandi67 – 726
    Helixi87 – 893
    Helixi91 – 10515
    Beta strandi109 – 1146
    Helixi116 – 1183
    Helixi121 – 13212
    Turni133 – 1364
    Beta strandi141 – 1455
    Helixi150 – 16617
    Helixi172 – 1743
    Helixi177 – 1804
    Helixi181 – 1833
    Turni185 – 1884
    Beta strandi193 – 1975
    Turni209 – 2146
    Beta strandi216 – 2194
    Helixi224 – 2263
    Helixi229 – 23911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F75X-ray2.20A/B1-249[»]
    ProteinModelPortaliO82827.
    SMRiO82827. Positions 14-242.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO82827.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 334Substrate binding
    Regioni74 – 763Substrate bindingBy similarity
    Regioni203 – 2053Substrate bindingBy similarity

    Domaini

    This enzyme shows a novel protein fold completely different from the "isoprenoid synthase fold" that is thought to be a common structure for the enzymes relating to isoprenoid biosynthesis.

    Sequence similaritiesi

    Belongs to the UPP synthase family.Curated

    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.

    O82827-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFPIKKRKAI KNNNINAAQI PKHIAIIMDG NGRWAKQKKM PRIKGHYEGM    50
    QTVKKITRYA SDLGVKYLTL YAFSTENWSR PKDEVNYLMK LPGDFLNTFL 100
    PELIEKNVKV ETIGFIDDLP DHTKKAVLEA KEKTKHNTGL TLVFALNYGG 150
    RKEIISAVQL IAERYKSGEI SLDEISETHF NEYLFTANMP DPELLIRTSG 200
    EERLSNFLIW QCSYSEFVFI DEFWPDFNEE SLAQCISIYQ NRHRRFGGL 249
    Length:249
    Mass (Da):28,876
    Last modified:November 1, 1998 - v1
    Checksum:i044F7DD77745AEEE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004319 Genomic DNA. Translation: BAA31993.1.
    PIRiT48857.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004319 Genomic DNA. Translation: BAA31993.1 .
    PIRi T48857.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F75 X-ray 2.20 A/B 1-249 [» ]
    ProteinModelPortali O82827.
    SMRi O82827. Positions 14-242.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei O82827.

    Family and domain databases

    Gene3Di 3.40.1180.10. 1 hit.
    HAMAPi MF_01139. ISPT.
    InterProi IPR001441. UPP_synth-like.
    IPR018520. UPP_synth-like_CS.
    [Graphical view ]
    PANTHERi PTHR10291. PTHR10291. 1 hit.
    Pfami PF01255. Prenyltransf. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64005. SSF64005. 1 hit.
    TIGRFAMsi TIGR00055. uppS. 1 hit.
    PROSITEi PS01066. UPP_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases."
      Shimizu N., Koyama T., Ogura K.
      J. Biol. Chem. 273:19476-19481(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION AS AN UNDECAPRENYL DIPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY.
      Strain: B-P 26.
    2. "Undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26: essential factors for the enzymatic activity."
      Koyama T., Yoshida I., Ogura K.
      J. Biochem. 103:867-871(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN UNDECAPRENYL DIPHOSPHATE SYNTHASE.
      Strain: B-P 26.
    3. "Significance of Asn-77 and Trp-78 in the catalytic function of undecaprenyl diphosphate synthase of Micrococcus luteus B-P 26."
      Fujikura K., Zhang Y.W., Yoshizaki H., Nishino T., Koyama T.
      J. Biochem. 128:917-922(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-77 AND TRP-78.
      Strain: B-P 26.
    4. "Identification of Significant residues for homoallylic substrate binding of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase."
      Kharel Y., Zhang Y.W., Fujihashi M., Miki K., Koyama T.
      J. Biol. Chem. 276:28459-28464(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PHE-73; SER-74; GLU-193; ARG-197; GLU-201; ARG-203; GLU-216; ASP-221 AND ASP-226.
      Strain: B-P 26.
    5. "Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase."
      Fujikura K., Zhang Y.-W., Fujihashi M., Miki K., Koyama T.
      Biochemistry 42:4035-4041(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-29; GLY-32; ARG-33; ARG-42; GLU-76; ARG-80 AND GLU-84.
      Strain: B-P 26.
    6. "Crystallization and preliminary X-ray diffraction studies of undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26."
      Fujihashi M., Shimizu N., Zhang Y.W., Koyama T., Miki K.
      Acta Crystallogr. D 55:1606-1607(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
      Strain: B-P 26.
    7. "Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase."
      Fujihashi M., Zhang Y.-W., Higuchi Y., Li X.-Y., Koyama T., Miki K.
      Proc. Natl. Acad. Sci. U.S.A. 98:4337-4342(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT.
      Strain: B-P 26.

    Entry informationi

    Entry nameiUPPS_MICLU
    AccessioniPrimary (citable) accession number: O82827
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 81 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, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3