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O82827

- UPPS_MICLU

UniProt

O82827 - UPPS_MICLU

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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

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
Complete GO annotation...

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

        10         20         30         40         50
MFPIKKRKAI KNNNINAAQI PKHIAIIMDG NGRWAKQKKM PRIKGHYEGM
60 70 80 90 100
QTVKKITRYA SDLGVKYLTL YAFSTENWSR PKDEVNYLMK LPGDFLNTFL
110 120 130 140 150
PELIEKNVKV ETIGFIDDLP DHTKKAVLEA KEKTKHNTGL TLVFALNYGG
160 170 180 190 200
RKEIISAVQL IAERYKSGEI SLDEISETHF NEYLFTANMP DPELLIRTSG
210 220 230 240
EERLSNFLIW QCSYSEFVFI DEFWPDFNEE SLAQCISIYQ NRHRRFGGL
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