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Reviewed, UniProtKB/Swiss-Prot Q92250 (FPPS_NEUCR)

Last modified January 19, 2010. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Farnesyl pyrophosphate synthetase
      Short name=FPP synthetase
      Short name=FPS
Alternative name(s):
    Farnesyl diphosphate synthetase
Including the following 2 domains:
    1- Recommended name:
            Dimethylallyltranstransferase
              EC=2.5.1.1
    2- Recommended name:
            Geranyltranstransferase
              EC=2.5.1.10
Gene names
Name: fpp
Synonyms: fpps
ORF Names: 123A4.020, NCU01175
OrganismNeurospora crassa [Complete proteome]
Taxonomic identifier5141 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

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Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.

Catalytic activity

Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.

Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Pathway

Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.

Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FPP/GGPP synthetase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Farnesyl pyrophosphate synthetase
PRO_0000123950

Sites

Metal binding951Magnesium 1 By similarity
Metal binding951Magnesium 2 By similarity
Metal binding991Magnesium 1 By similarity
Metal binding991Magnesium 2 By similarity
Metal binding2351Magnesium 3 By similarity
Binding site501Isopentenyl diphosphate By similarity
Binding site531Isopentenyl diphosphate By similarity
Binding site881Isopentenyl diphosphate By similarity
Binding site1041Dimethylallyl diphosphate By similarity
Binding site1051Isopentenyl diphosphate By similarity
Binding site1921Dimethylallyl diphosphate By similarity
Binding site1931Dimethylallyl diphosphate By similarity
Binding site2321Dimethylallyl diphosphate By similarity
Binding site2491Dimethylallyl diphosphate By similarity
Binding site2581Dimethylallyl diphosphate By similarity

Experimental info

Sequence conflict1341L → R in CAA65645. Ref.1
Sequence conflict3211I → N in CAA65645. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q92250-1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 83F4DC7C4D61212F

FASTA34740,278
        10         20         30         40         50         60 
MAKTTTLKEF ESVFPKLEEA LLEYAKAYKL PEQMLSWYKQ SLEVNTLGGK CNRGMSVPDS 

        70         80         90        100        110        120 
ASILLGRPLT EEEYFQAATL GWMTELLQAF FLVSDDIMDS SITRRGKPCW YRQEGVGMVA 

       130        140        150        160        170        180 
INDAFMLESA IYTLLKKYFR SHPRYVDFLE LFHEVTFQTE MGQLCDLLTA PEDKVDLDNF 

       190        200        210        220        230        240 
SMDKYTFIVI YKTAYYSFYL PVALAMYMLD IATPENLKQA EDILIPLGEY FQVQDDYLDN 

       250        260        270        280        290        300 
FGLPEHIGKI GTDIQDNKCS WLVNKALSIV TPEQRKTLEE NYGRKDKAKE AVIKQLYDDL 

       310        320        330        340 
KLEDHYKQYE EERVGEIRKM IDAIDESKGL KKQVFEAFLG KIYKRSK

« Hide

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References

« Hide 'large scale' references
[1]"The isoprenoid pathway: cloning and characterization of fungal FPPS genes."
Homann V., Mende K., Arntz C., Ilardi V., Macino G., Morelli G., Bose G., Tudzynski B.
Curr. Genet. 30:232-239(1996) [PubMed: 8753652] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[2]"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]"The genome sequence of the filamentous fungus Neurospora crassa."
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. expand/collapse author list , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
Nature 422:859-868(2003) [PubMed: 12712197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X96944 Genomic DNA. Translation: CAA65645.1.
AL670009 Genomic DNA. Translation: CAD21355.1.
AABX02000015 Genomic DNA. Translation: EAA32305.1.
PIRS71436.
RefSeqXP_961541.1.

3D structure databases

SMRQ92250. Positions 6-347.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ92250.

Genome annotation databases

GeneID3877737.
KEGGncr:NCU01175.
NMPDRfig|5141.1.peg.4601.

Phylogenomic databases

OrthoDBEOG9D286Q.
PhylomeDBQ92250.

Enzyme and pathway databases

BRENDA2.5.1.1. 266.
2.5.1.10. 266.

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
PROSITEPS00723. POLYPRENYL_SYNTHET_1. 1 hit.
PS00444. POLYPRENYL_SYNTHET_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameFPPS_NEUCR
AccessionPrimary (citable) accession number: Q92250
Secondary accession number(s): Q1K859, Q8X0Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 7, 2005
Last modified: January 19, 2010
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents