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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei40 – 401By similarity
Metal bindingi40 – 401MagnesiumBy similarity
Binding sitei45 – 451SubstrateBy similarity
Sitei84 – 841Important for determining product length
Active sitei89 – 891Proton acceptor
Binding sitei92 – 921SubstrateBy similarity
Binding sitei211 – 2111Substrate
Metal bindingi230 – 2301MagnesiumBy similarity

GO - Molecular functioni

  • magnesium ion binding Source: MTBBASE
  • manganese ion binding Source: MTBBASE
  • prenyltransferase activity Source: UniProtKB-HAMAP
  • 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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi84 – 841L → 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 Publications
Mutagenesisi107 – 1071V → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262(2Z,6E)-farnesyl diphosphate synthasePRO_0000123748Add
BLAST

Proteomic databases

PaxDbiP9WFF5.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv1086.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 386Combined sources
Helixi42 – 487Combined sources
Helixi55 – 7521Combined sources
Beta strandi78 – 869Combined sources
Helixi88 – 914Combined sources
Helixi94 – 11118Combined sources
Turni114 – 1163Combined sources
Beta strandi119 – 1246Combined sources
Helixi126 – 1283Combined sources
Helixi131 – 14212Combined sources
Beta strandi151 – 1588Combined sources
Helixi160 – 17718Combined sources
Helixi182 – 1887Combined sources
Helixi191 – 1977Combined sources
Turni199 – 2024Combined sources
Beta strandi207 – 2115Combined sources
Turni219 – 22810Combined sources
Beta strandi230 – 2334Combined sources
Helixi238 – 2403Combined sources
Helixi243 – 25513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VFWX-ray2.30A/B30-256[»]
2VG0X-ray1.70A/B30-256[»]
2VG1X-ray1.70A/B29-256[»]
ProteinModelPortaliP9WFF5.
SMRiP9WFF5. Positions 29-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 444Substrate binding
Regioni86 – 883Substrate binding
Regioni217 – 2193Substrate binding

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2VFWX-ray2.30A/B30-256[»]
2VG0X-ray1.70A/B30-256[»]
2VG1X-ray1.70A/B29-256[»]
ProteinModelPortaliP9WFF5.
SMRiP9WFF5. Positions 29-256.
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.

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: 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.