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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: 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

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei291
Metal bindingi29MagnesiumBy similarity1
Binding sitei34SubstrateBy similarity1
Binding sitei42Substrate1
Binding sitei46SubstrateBy similarity1
Active sitei77Proton acceptorBy similarity1
Binding sitei78SubstrateBy similarity1
Binding sitei80SubstrateBy similarity1
Binding sitei197SubstrateBy similarity1
Metal bindingi216MagnesiumBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi2.5.1.31. 3348.

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 lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeMicrococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29D → A: Great decrease in activity. 1 Publication1
Mutagenesisi32G → R: Great decrease in activity. Decrease in activity; when associated with G-42. 1 Publication1
Mutagenesisi33R → A: Decrease in affinity for decaprenyl diphosphate substrate analog. 1 Publication1
Mutagenesisi42R → G: Great decrease in activity. Decrease in activity; when associated with R-32. 1 Publication1
Mutagenesisi73F → A: Decrease in activity; reduced affinity for substrate. 1 Publication1
Mutagenesisi74S → A: Decrease in activity; reduced affinity for substrate. 1 Publication1
Mutagenesisi76E → Q: Slight decrease in activity. 1 Publication1
Mutagenesisi77N → A, D or Q: Great decrease in activity. 1 Publication1
Mutagenesisi78W → I, R or D: Decrease in activity. 1 Publication1
Mutagenesisi80R → A: Great decrease in activity. 1 Publication1
Mutagenesisi84E → Q: Slight decrease in activity. 1 Publication1
Mutagenesisi193E → Q: Decrease in activity. 1 Publication1
Mutagenesisi197R → S: Great decrease in activity; reduced affinity for substrate. 1 Publication1
Mutagenesisi201E → Q: Slight decrease in activity. 1 Publication1
Mutagenesisi203R → S: Great decrease in activity; reduced affinity for substrate. 1 Publication1
Mutagenesisi216E → Q: Great decrease in activity; reduced affinity for substrate. 1 Publication1
Mutagenesisi221D → A: Decrease in activity. 1 Publication1
Mutagenesisi226D → A: Slight decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001236371 – 249Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)Add BLAST249

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1249
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 28Combined sources7
Helixi31 – 37Combined sources7
Helixi42 – 63Combined sources22
Beta strandi67 – 72Combined sources6
Helixi87 – 89Combined sources3
Helixi91 – 105Combined sources15
Beta strandi109 – 114Combined sources6
Helixi116 – 118Combined sources3
Helixi121 – 132Combined sources12
Turni133 – 136Combined sources4
Beta strandi141 – 145Combined sources5
Helixi150 – 166Combined sources17
Helixi172 – 174Combined sources3
Helixi177 – 180Combined sources4
Helixi181 – 183Combined sources3
Turni185 – 188Combined sources4
Beta strandi193 – 197Combined sources5
Turni209 – 214Combined sources6
Beta strandi216 – 219Combined sources4
Helixi224 – 226Combined sources3
Helixi229 – 239Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F75X-ray2.20A/B1-249[»]
ProteinModelPortaliO82827.
SMRiO82827.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO82827.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 33Substrate binding4
Regioni74 – 76Substrate bindingBy similarity3
Regioni203 – 205Substrate bindingBy similarity3

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

Phylogenomic databases

KOiK00806.

Family and domain databases

CDDicd00475. Cis_IPPS. 1 hit.
Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT. 1 hit.
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:
EMBLi
GenBanki
DDBJi
Links Updated
AB004319 Genomic DNA. Translation: BAA31993.1.
PIRiT48857.

Genome annotation databases

KEGGiag:BAA31993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004319 Genomic DNA. Translation: BAA31993.1.
PIRiT48857.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F75X-ray2.20A/B1-249[»]
ProteinModelPortaliO82827.
SMRiO82827.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA31993.

Phylogenomic databases

KOiK00806.

Enzyme and pathway databases

BRENDAi2.5.1.31. 3348.

Miscellaneous databases

EvolutionaryTraceiO82827.

Family and domain databases

CDDicd00475. Cis_IPPS. 1 hit.
Gene3Di3.40.1180.10. 1 hit.
HAMAPiMF_01139. ISPT. 1 hit.
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...

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: November 30, 2016
This is version 91 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

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.