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Q08291 (ISPA_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Farnesyl diphosphate synthase
Short name=FPP synthase
EC=2.5.1.10
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Geranyltranstransferase
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Ontologies

Keywords
   Biological processIsoprene biosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processisoprenoid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiongeranyltranstransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Farnesyl diphosphate synthase
PRO_0000123985

Sites

Metal binding861Magnesium 1 By similarity
Metal binding861Magnesium 2 By similarity
Metal binding921Magnesium 1 By similarity
Metal binding921Magnesium 2 By similarity
Metal binding2241Magnesium 3 By similarity
Binding site471Isopentenyl diphosphate By similarity
Binding site501Isopentenyl diphosphate By similarity
Binding site791Isopentenyl diphosphate By similarity
Binding site971Geranyl diphosphate By similarity
Binding site981Isopentenyl diphosphate By similarity
Binding site1831Geranyl diphosphate By similarity
Binding site1841Geranyl diphosphate By similarity
Binding site2211Geranyl diphosphate By similarity
Binding site2381Geranyl diphosphate By similarity

Experimental info

Mutagenesis731C → F or S: No loss of activity. Ref.2
Mutagenesis2891C → F or S: No loss of activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q08291 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 0F921C3F029EEBB6

FASTA29732,310
        10         20         30         40         50         60 
MAQLSVEQFL NEQKQAVETA LSRYIERLEG PAKLKKAMAY SLEAGGKRIR PLLLLSTVRA 

        70         80         90        100        110        120 
LGKDPAVGLP VACAIEMIHT YSLIHDDLPS MDNDDLRRGK PTNHKVFGEA MAILAGDGLL 

       130        140        150        160        170        180 
TYAFQLITEI DDERIPPSVR LRLIERLAKA AGPEGMVAGQ AADMEGEGKT LTLSELEYIH 

       190        200        210        220        230        240 
RHKTGKMLQY SVHAGALIGG ADARQTRELD EFAAHLGLAF QIRDDILDIE GAEEKIGKPV 

       250        260        270        280        290 
GSDQSNNKAT YPALLSLAGA KEKLAFHIEA AQRHLRNADV DGAALAYICE LVAARDH

« Hide

References

[1]"Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: molecular cloning, sequence determination, overproduction, and purification."
Koyama T., Obata S., Osabe M., Takeshita A., Yokoyama K., Uchida M., Nishino T., Ogura K.
J. Biochem. 113:355-363(1993) [PubMed: 8486607] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 10149 / DSM 6790 / JCM 11297 / NRS T15.
[2]"Structural and functional roles of the cysteine residues of Bacillus stearothermophilus farnesyl diphosphate synthase."
Koyama T., Obata S., Saito K., Takeshita-Koike A., Ogura K.
Biochemistry 33:12644-12648(1994) [PubMed: 7918490] [Abstract]
Cited for: MUTAGENESIS OF CYSTEINE RESIDUES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D13293 Genomic DNA. Translation: BAA02551.1.
S72629 Genomic DNA. Translation: AAB32272.1.
S72630 Genomic DNA. Translation: AAB32273.2. Sequence problems.
S72633 Genomic DNA. Translation: AAB32274.1.
S72635 Genomic DNA. Translation: AAB32275.2. Sequence problems.
PIRJX0257.

3D structure databases

ProteinModelPortalQ08291.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
PANTHERPTHR12001. Polyprenyl_synt. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. Terpenoid_synth. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPA_GEOSE
AccessionPrimary (citable) accession number: Q08291
Secondary accession number(s): Q53435 expand/collapse secondary AC list , Q53436, Q53437, Q53438
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: September 21, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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