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Q92250 (FPPS_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Farnesyl pyrophosphate synthase
Short name=FPP synthase
Short name=FPS
EC=2.5.1.10
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase
EC=2.5.1.1
Farnesyl diphosphate synthase
Geranyltranstransferase
Gene names
Name:fpp
Synonyms:fpps
ORF Names:123A4.020, NCU01175
OrganismNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]
Taxonomic identifier367110 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora ›

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 + (2E,6E)-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 synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Farnesyl pyrophosphate synthase
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

Sequences

Sequence LengthMass (Da)Tools
Q92250 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

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. XM_956448.1.
UniGeneNcr.15758.

3D structure databases

ProteinModelPortalQ92250.
ModBaseSearch...

Protein-protein interaction databases

STRING5141.NCU01175.1.

Proteomic databases

PRIDEQ92250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiEFNCRT00000004433; EFNCRP00000004433; EFNCRG00000004427.
GeneID3877737.
KEGGncr:NCU01175.

Phylogenomic databases

eggNOGCOG0142.
HOGENOMHOG000160912.
KOK00787.
OMAVAMQRAN.
OrthoDBEOG4SFDFW.

Enzyme and pathway databases

UniPathwayUPA00259; UER00368.
UPA00260; UER00369.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
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 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: April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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