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

Farnesyl diphosphate synthase

Gene

ispA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 3 Mg2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45Isopentenyl diphosphate1 Publication1
Binding sitei48Isopentenyl diphosphate1 Publication1
Binding sitei77Isopentenyl diphosphate1 Publication1
Metal bindingi84Magnesium 11 Publication1
Metal bindingi84Magnesium 21 Publication1
Metal bindingi90Magnesium 11 Publication1
Metal bindingi90Magnesium 21 Publication1
Binding sitei95Geranyl diphosphate1
Binding sitei96Isopentenyl diphosphate1 Publication1
Binding sitei181Geranyl diphosphate1
Binding sitei182Geranyl diphosphate1
Binding sitei220Geranyl diphosphate1
Metal bindingi223Magnesium 31 Publication1
Binding sitei237Geranyl diphosphate1

GO - Molecular functioni

  • dimethylallyltranstransferase activity Source: EcoCyc
  • geranyltranstransferase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • farnesyl diphosphate biosynthetic process Source: EcoCyc
  • geranyl diphosphate biosynthetic process Source: EcoCyc

Keywordsi

Molecular functionTransferase
Biological processIsoprene biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:FPPSYN-MONOMER.
MetaCyc:FPPSYN-MONOMER.
SABIO-RKiP22939.

Names & Taxonomyi

Protein namesi
Recommended name:
Farnesyl diphosphate synthase (EC:2.5.1.10)
Short name:
FPP synthase
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Geranyltranstransferase
Gene namesi
Name:ispA
Ordered Locus Names:b0421, JW0411
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10508. ispA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075078.
DrugBankiDB02270. Dimethylallyl S-Thiolodiphosphate.
DB04160. Diphosphate.
DB02508. Isopentyl Pyrophosphate.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001239821 – 299Farnesyl diphosphate synthaseAdd BLAST299

Proteomic databases

PaxDbiP22939.
PRIDEiP22939.

2D gel databases

SWISS-2DPAGEiP22939.

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4259837. 457 interactors.
DIPiDIP-10044N.
IntActiP22939. 16 interactors.
MINTiMINT-1233182.
STRINGi316385.ECDH10B_0377.

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 22Combined sources20
Beta strandi25 – 27Combined sources3
Helixi31 – 41Combined sources11
Helixi47 – 58Combined sources12
Helixi63 – 84Combined sources22
Turni87 – 90Combined sources4
Helixi101 – 105Combined sources5
Helixi107 – 127Combined sources21
Helixi135 – 149Combined sources15
Helixi154 – 163Combined sources10
Turni164 – 167Combined sources4
Helixi171 – 181Combined sources11
Helixi183 – 195Combined sources13
Turni196 – 198Combined sources3
Helixi199 – 229Combined sources31
Helixi232 – 235Combined sources4
Helixi241 – 245Combined sources5
Helixi250 – 254Combined sources5
Helixi256 – 278Combined sources23
Turni279 – 281Combined sources3
Helixi285 – 296Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RQIX-ray2.42A/B1-299[»]
1RQJX-ray1.95A/B1-299[»]
ProteinModelPortaliP22939.
SMRiP22939.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22939.

Family & Domainsi

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105CTB. Bacteria.
COG0142. LUCA.
HOGENOMiHOG000009101.
InParanoidiP22939.
KOiK00795.
PhylomeDBiP22939.

Family and domain databases

Gene3Di1.10.600.10. 2 hits.
InterProiView protein in InterPro
IPR008949. Isoprenoid_synthase_dom.
IPR000092. Polyprenyl_synt.
IPR033749. Polyprenyl_synt_CS.
PfamiView protein in Pfam
PF00348. polyprenyl_synt. 1 hit.
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiView protein in PROSITE
PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P22939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFPQQLEAC VKQANQALSR FIAPLPFQNT PVVETMQYGA LLGGKRLRPF
60 70 80 90 100
LVYATGHMFG VSTNTLDAPA AAVECIHAYS LIHDDLPAMD DDDLRRGLPT
110 120 130 140 150
CHVKFGEANA ILAGDALQTL AFSILSDADM PEVSDRDRIS MISELASASG
160 170 180 190 200
IAGMCGGQAL DLDAEGKHVP LDALERIHRH KTGALIRAAV RLGALSAGDK
210 220 230 240 250
GRRALPVLDK YAESIGLAFQ VQDDILDVVG DTATLGKRQG ADQQLGKSTY
260 270 280 290
PALLGLEQAR KKARDLIDDA RQSLKQLAEQ SLDTSALEAL ADYIIQRNK
Length:299
Mass (Da):32,160
Last modified:August 1, 1991 - v1
Checksum:i15BADD5E135060CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00694 Genomic DNA. Translation: BAA00599.1.
U82664 Genomic DNA. Translation: AAB40177.1.
U00096 Genomic DNA. Translation: AAC73524.1.
AP009048 Genomic DNA. Translation: BAE76201.1.
PIRiJQ0665.
RefSeqiNP_414955.1. NC_000913.3.
WP_000347217.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73524; AAC73524; b0421.
BAE76201; BAE76201; BAE76201.
GeneIDi945064.
KEGGiecj:JW0411.
eco:b0421.
PATRICifig|1411691.4.peg.1856.

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.

Entry informationi

Entry nameiISPA_ECOLI
AccessioniPrimary (citable) accession number: P22939
Secondary accession number(s): Q2MC05
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 5, 2017
This is version 143 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families