Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Decaprenyl diphosphate synthase

Gene

uppS

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) in the cis configuration with (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP) generating the 50 carbon product trans,polycis-decaprenyl diphosphate. When (2E,6E)-farnesyl diphosphate (E-FPP or EE-FPP) is used in vitro, both primary products decaprenyl diphosphate and (2E,6E,10E)-geranylgeranyl diphosphate (EEE-GGPP) are synthesized. M.tuberculosis does not synthesize (2E,6E,10Z)-geranylgeranyl diphosphate (EEZ-GGPP) and heptaprenyl diphosphate. Can also accept many different allylic substrates, including E-geranyl diphosphate (E-GPP), neryl diphosphate (NPP), and all-trans-geranyl-geranyl diphosphate.3 Publications

Catalytic activityi

(2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate.
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55).

Cofactori

Mg2+2 Publications, Mn2+2 PublicationsNote: Binds 2 magnesium ions per subunit. Can also use manganese as divalent cation, however calcium and zinc ions are much less effective.2 Publications

Enzyme regulationi

Activated by dithiothreitol and inhibited by EDTA.1 Publication

Kineticsi

  1. KM=29 µM for NPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  2. KM=40 µM for EEE-GGPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  3. KM=84 µM for EE-FPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  4. KM=89 µM for IPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  5. KM=290 µM for EZ-FPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  6. KM=490 µM for E-GPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  1. Vmax=12 pmol/min/mg enzyme with EEE-GGPP as substrate (at pH 7.9 and 37 degrees Celsius)1 Publication
  2. Vmax=21 pmol/min/mg enzyme with NPP as substrate (at pH 7.9 and 37 degrees Celsius)1 Publication
  3. Vmax=25 pmol/min/mg enzyme with E-GPP as substrate (at pH 7.9 and 37 degrees Celsius)1 Publication
  4. Vmax=30 pmol/min/mg enzyme with EE-FPP as substrate (at pH 7.9 and 37 degrees Celsius)1 Publication
  5. Vmax=4800 pmol/min/mg enzyme with EZ-FPP as substrate (at pH 7.9 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 7.5 and 8.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei76 – 761By similarity
Metal bindingi76 – 761MagnesiumBy similarity
Binding sitei81 – 811SubstrateBy similarity
Binding sitei89 – 891Substrate
Binding sitei93 – 931SubstrateBy similarity
Active sitei124 – 1241Proton acceptor
Binding sitei125 – 1251SubstrateBy similarity
Binding sitei127 – 1271Substrate
Binding sitei168 – 1681Substrate
Binding sitei244 – 2441Substrate
Metal bindingi263 – 2631MagnesiumBy similarity

GO - Molecular functioni

  • di-trans,poly-cis-decaprenylcistransferase activity Source: MTBBASE
  • magnesium ion binding Source: MTBBASE
  • manganese ion binding Source: MTBBASE
  • trans-octaprenyltranstransferase activity Source: MTBBASE
  • Z-farnesyl diphosphate synthase activity Source: MTBBASE

GO - Biological processi

  • growth Source: MTBBASE
  • polyprenol biosynthetic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Decaprenyl diphosphate synthase (EC:2.5.1.86, EC:2.5.1.87)
Short name:
DecaPP
Alternative name(s):
Decaprenyl pyrophosphate synthase
Long-chain isoprenyl diphosphate synthase
Trans,polycis-decaprenyl diphosphate synthase
Gene namesi
Name:uppS
Ordered Locus Names:Rv2361c
ORF Names:MTCY27.19
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2361c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Decaprenyl diphosphate synthasePRO_0000123641Add
BLAST

Proteomic databases

PaxDbiP9WFF7.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2361c.

Structurei

Secondary structure

1
296
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Beta strandi43 – 464Combined sources
Turni64 – 663Combined sources
Beta strandi69 – 746Combined sources
Helixi78 – 847Combined sources
Helixi89 – 11022Combined sources
Beta strandi114 – 1218Combined sources
Helixi124 – 1263Combined sources
Helixi129 – 15224Combined sources
Beta strandi155 – 1617Combined sources
Helixi168 – 18114Combined sources
Beta strandi186 – 19510Combined sources
Helixi197 – 21317Combined sources
Helixi219 – 2213Combined sources
Helixi224 – 2307Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi240 – 2445Combined sources
Turni252 – 26110Combined sources
Beta strandi263 – 2664Combined sources
Helixi271 – 2733Combined sources
Helixi276 – 28813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VG2X-ray1.95A/B/C/D13-296[»]
2VG3X-ray1.80A/B/C/D13-296[»]
2VG4X-ray2.60A/B/C/D13-296[»]
4ONCX-ray1.83A/B13-296[»]
ProteinModelPortaliP9WFF7.
SMRiP9WFF7. Positions 13-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 805Substrate binding
Regioni121 – 1244Substrate binding
Regioni250 – 2523Substrate binding
Regioni292 – 2943Substrate binding

Sequence similaritiesi

Belongs to the UPP synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105CR3. Bacteria.
COG0020. LUCA.
KOiK14215.
OMAiWNRPKLE.
PhylomeDBiP9WFF7.

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.

P9WFF7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARDARKRTS SNFPQLPPAP DDYPTFPDTS TWPVVFPELP AAPYGGPCRP
60 70 80 90 100
PQHTSKAAAP RIPADRLPNH VAIVMDGNGR WATQRGLART EGHKMGEAVV
110 120 130 140 150
IDIACGAIEL GIKWLSLYAF STENWKRSPE EVRFLMGFNR DVVRRRRDTL
160 170 180 190 200
KKLGVRIRWV GSRPRLWRSV INELAVAEEM TKSNDVITIN YCVNYGGRTE
210 220 230 240 250
ITEATREIAR EVAAGRLNPE RITESTIARH LQRPDIPDVD LFLRTSGEQR
260 270 280 290
SSNFMLWQAA YAEYIFQDKL WPDYDRRDLW AACEEYASRT RRFGSA
Length:296
Mass (Da):33,791
Last modified:April 16, 2014 - v1
Checksum:i93895E54253615AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45149.1.
PIRiH70585.
RefSeqiNP_216877.1. NC_000962.3.
WP_003412212.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45149; CCP45149; Rv2361c.
GeneIDi888964.
KEGGimtu:Rv2361c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45149.1.
PIRiH70585.
RefSeqiNP_216877.1. NC_000962.3.
WP_003412212.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VG2X-ray1.95A/B/C/D13-296[»]
2VG3X-ray1.80A/B/C/D13-296[»]
2VG4X-ray2.60A/B/C/D13-296[»]
4ONCX-ray1.83A/B13-296[»]
ProteinModelPortaliP9WFF7.
SMRiP9WFF7. Positions 13-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2361c.

Proteomic databases

PaxDbiP9WFF7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45149; CCP45149; Rv2361c.
GeneIDi888964.
KEGGimtu:Rv2361c.

Organism-specific databases

TubercuListiRv2361c.

Phylogenomic databases

eggNOGiENOG4105CR3. Bacteria.
COG0020. LUCA.
KOiK14215.
OMAiWNRPKLE.
PhylomeDBiP9WFF7.

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 nameiDPDS_MYCTU
AccessioniPrimary (citable) accession number: P9WFF7
Secondary accession number(s): L0T9E4, O05837, P60479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: September 7, 2016
This is version 16 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. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  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.