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Protein

(2Z,6E)-farnesyl diphosphate synthase

Gene

Rv1086

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 condensation of only one isopentenyl pyrophosphate (IPP) unit in the cis configuration to E-geranyl diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl diphosphate (Z-FPP or EZ-FPP). Z-FPP is the precursor of decaprenyl diphosphate, which has a central role in the biosynthesis of the mycobacterial cell wall.3 Publications

Catalytic activityi

Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2Z,6E)-farnesyl diphosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit.1 Publication

Enzyme regulationi

Inhibited by citronellyl diphosphate.1 Publication

Kineticsi

  1. KM=16 µM for neryl diphosphate (at pH 7.9 and 37 degrees Celsius)1 Publication
  2. KM=38 µM for E-GPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  3. KM=124 µM for IPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  1. Vmax=4328 pmol/min/mg enzyme for IPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  2. Vmax=2827 pmol/min/mg enzyme for E-GPP (at pH 7.9 and 37 degrees Celsius)1 Publication
  3. Vmax=1098 pmol/min/mg enzyme for neryl diphosphate (at pH 7.9 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 7 and 8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei40By similarity1
Metal bindingi40MagnesiumBy similarity1
Binding sitei45SubstrateBy similarity1
Sitei84Important for determining product length1
Active sitei89Proton acceptor1
Binding sitei92SubstrateBy similarity1
Binding sitei211Substrate1
Metal bindingi230MagnesiumBy similarity1

GO - Molecular functioni

  • magnesium ion binding Source: MTBBASE
  • manganese ion binding Source: MTBBASE
  • polyprenyltransferase activity Source: GO_Central
  • Z-farnesyl diphosphate synthase activity Source: MTBBASE

GO - Biological processi

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

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:G185E-5248-MONOMER.
MTBH37RV:G185E-5248-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
(2Z,6E)-farnesyl diphosphate synthase (EC:2.5.1.68)
Alternative name(s):
Short-chain Z-isoprenyl diphosphate synthase
Z-FPP synthase
Short name:
Z-FPPS
Z-Polyprenyl diphosphate synthase
Z-isoprenyl diphosphate synthase
Gene namesi
Ordered Locus Names:Rv1086
ORF Names:MTV017.39
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1086.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi84L → A: 4-fold decrease in affinity relative to the wild-type and able to synthesize prenyl diphosphates containing 20 and 50 carbon atoms when GPP and EE-FPP are used as the allylic substrates, respectively, whereas the wild-type enzyme generates product that is restricted to 15 carbon atoms with GPP as substrate and does not react with EE-FPP; when associated with G-107. 2 Publications1
Mutagenesisi107V → G: No detectable activity. 4-fold decrease in affinity relative to the wild-type and able to synthesize prenyl diphosphates containing 20 and 50 carbon atoms when GPP and EE-FPP are used as the allylic substrates, respectively, whereas the wild-type enzyme generates product that is restricted to 15 carbon atoms with GPP as substrate and does not react with EE-FPP; when associated with A-84. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001237481 – 262(2Z,6E)-farnesyl diphosphate synthaseAdd BLAST262

Proteomic databases

PaxDbiP9WFF5.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv1086.

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 38Combined sources6
Helixi42 – 48Combined sources7
Helixi55 – 75Combined sources21
Beta strandi78 – 86Combined sources9
Helixi88 – 91Combined sources4
Helixi94 – 111Combined sources18
Turni114 – 116Combined sources3
Beta strandi119 – 124Combined sources6
Helixi126 – 128Combined sources3
Helixi131 – 142Combined sources12
Beta strandi151 – 158Combined sources8
Helixi160 – 177Combined sources18
Helixi182 – 188Combined sources7
Helixi191 – 197Combined sources7
Turni199 – 202Combined sources4
Beta strandi207 – 211Combined sources5
Turni219 – 228Combined sources10
Beta strandi230 – 233Combined sources4
Helixi238 – 240Combined sources3
Helixi243 – 255Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VFWX-ray2.30A/B30-256[»]
2VG0X-ray1.70A/B30-256[»]
2VG1X-ray1.70A/B29-256[»]
ProteinModelPortaliP9WFF5.
SMRiP9WFF5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 44Substrate binding4
Regioni86 – 88Substrate binding3
Regioni217 – 219Substrate binding3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CR3. Bacteria.
COG0020. LUCA.
KOiK12503.
OMAiHINLAVG.
PhylomeDBiP9WFF5.

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.

P9WFF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIIPPRLKE PLYRLYELRL RQGLAASKSD LPRHIAVLCD GNRRWARSAG
60 70 80 90 100
YDDVSYGYRM GAAKIAEMLR WCHEAGIELA TVYLLSTENL QRDPDELAAL
110 120 130 140 150
IEIITDVVEE ICAPANHWSV RTVGDLGLIG EEPARRLRGA VESTPEVASF
160 170 180 190 200
HVNVAVGYGG RREIVDAVRA LLSKELANGA TAEELVDAVT VEGISENLYT
210 220 230 240 250
SGQPDPDLVI RTSGEQRLSG FLLWQSAYSE MWFTEAHWPA FRHVDFLRAL
260
RDYSARHRSY GR
Length:262
Mass (Da):29,410
Last modified:April 16, 2014 - v1
Checksum:i2D6745748FE22518
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43837.1.
PIRiD70895.
RefSeqiNP_215602.1. NC_000962.3.
WP_003906511.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP43837; CCP43837; Rv1086.
GeneIDi887097.
KEGGimtu:Rv1086.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43837.1.
PIRiD70895.
RefSeqiNP_215602.1. NC_000962.3.
WP_003906511.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VFWX-ray2.30A/B30-256[»]
2VG0X-ray1.70A/B30-256[»]
2VG1X-ray1.70A/B29-256[»]
ProteinModelPortaliP9WFF5.
SMRiP9WFF5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1086.

Proteomic databases

PaxDbiP9WFF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43837; CCP43837; Rv1086.
GeneIDi887097.
KEGGimtu:Rv1086.

Organism-specific databases

TubercuListiRv1086.

Phylogenomic databases

eggNOGiENOG4105CR3. Bacteria.
COG0020. LUCA.
KOiK12503.
OMAiHINLAVG.
PhylomeDBiP9WFF5.

Enzyme and pathway databases

BioCyciMetaCyc:G185E-5248-MONOMER.
MTBH37RV:G185E-5248-MONOMER.

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 nameiZFPP_MYCTU
AccessioniPrimary (citable) accession number: P9WFF5
Secondary accession number(s): L0T8K3, O53434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 17 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.