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O82827 (UPPS_MICLU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:uppS
OrganismMicrococcus luteus (Micrococcus lysodeikticus)
Taxonomic identifier1270 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeMicrococcus

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per subunit By similarity. HAMAP-Rule MF_01139

Subunit structure

Homodimer. Ref.7

Domain

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. HAMAP-Rule MF_01139

Sequence similarities

Belongs to the UPP synthase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) HAMAP-Rule MF_01139
PRO_0000123637

Regions

Region30 – 334Substrate binding HAMAP-Rule MF_01139
Region74 – 763Substrate binding By similarity
Region203 – 2053Substrate binding By similarity

Sites

Active site291
Active site771Proton acceptor By similarity
Metal binding291Magnesium By similarity
Metal binding2161Magnesium By similarity
Binding site341Substrate By similarity
Binding site421Substrate
Binding site461Substrate By similarity
Binding site781Substrate By similarity
Binding site801Substrate By similarity
Binding site1971Substrate By similarity

Experimental info

Mutagenesis291D → A: Great decrease in activity. Ref.5
Mutagenesis321G → R: Great decrease in activity. Decrease in activity; when associated with G-42. Ref.5
Mutagenesis331R → A: Decrease in affinity for decaprenyl diphosphate substrate analog. Ref.5
Mutagenesis421R → G: Great decrease in activity. Decrease in activity; when associated with R-32. Ref.5
Mutagenesis731F → A: Decrease in activity; reduced affinity for substrate. Ref.4
Mutagenesis741S → A: Decrease in activity; reduced affinity for substrate. Ref.4
Mutagenesis761E → Q: Slight decrease in activity. Ref.5
Mutagenesis771N → A, D or Q: Great decrease in activity. Ref.3
Mutagenesis781W → I, R or D: Decrease in activity. Ref.3
Mutagenesis801R → A: Great decrease in activity. Ref.5
Mutagenesis841E → Q: Slight decrease in activity. Ref.5
Mutagenesis1931E → Q: Decrease in activity. Ref.4
Mutagenesis1971R → S: Great decrease in activity; reduced affinity for substrate. Ref.4
Mutagenesis2011E → Q: Slight decrease in activity. Ref.4
Mutagenesis2031R → S: Great decrease in activity; reduced affinity for substrate. Ref.4
Mutagenesis2161E → Q: Great decrease in activity; reduced affinity for substrate. Ref.4
Mutagenesis2211D → A: Decrease in activity. Ref.4
Mutagenesis2261D → A: Slight decrease in activity. Ref.4

Secondary structure

......................................... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O82827 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 044F7DD77745AEEE

FASTA24928,876
        10         20         30         40         50         60 
MFPIKKRKAI KNNNINAAQI PKHIAIIMDG NGRWAKQKKM PRIKGHYEGM QTVKKITRYA 

        70         80         90        100        110        120 
SDLGVKYLTL YAFSTENWSR PKDEVNYLMK LPGDFLNTFL PELIEKNVKV ETIGFIDDLP 

       130        140        150        160        170        180 
DHTKKAVLEA KEKTKHNTGL TLVFALNYGG RKEIISAVQL IAERYKSGEI SLDEISETHF 

       190        200        210        220        230        240 
NEYLFTANMP DPELLIRTSG EERLSNFLIW QCSYSEFVFI DEFWPDFNEE SLAQCISIYQ 


NRHRRFGGL 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB004319 Genomic DNA. Translation: BAA31993.1.
PIRT48857.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F75X-ray2.20A/B1-249[»]
ProteinModelPortalO82827.
SMRO82827. Positions 14-242.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.1180.10. 1 hit.
HAMAPMF_01139. ISPT.
InterProIPR001441. UPP_synth-like.
IPR018520. UPP_synth-like_CS.
[Graphical view]
PANTHERPTHR10291. PTHR10291. 1 hit.
PfamPF01255. Prenyltransf. 1 hit.
[Graphical view]
SUPFAMSSF64005. SSF64005. 1 hit.
TIGRFAMsTIGR00055. uppS. 1 hit.
PROSITEPS01066. UPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO82827.

Entry information

Entry nameUPPS_MICLU
AccessionPrimary (citable) accession number: O82827
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references