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Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase)

 FPPS_NEUCR              Reviewed;         347 AA.
Q92250; Q1K859; Q8X0Y6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
28-MAR-2018, entry version 113.
RecName: Full=Farnesyl pyrophosphate synthase;
Short=FPP synthase;
Short=FPS;
EC=2.5.1.10;
AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
AltName: Full=Dimethylallyltranstransferase;
EC=2.5.1.1;
AltName: Full=Farnesyl diphosphate synthase;
AltName: Full=Geranyltranstransferase;
Name=fpp; Synonyms=fpps; ORFNames=123A4.020, NCU01175;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=8753652; DOI=10.1007/s002940050126;
Homann V., Mende K., Arntz C., Ilardi V., Macino G., Morelli G.,
Bose G., Tudzynski B.;
"The isoprenoid pathway: cloning and characterization of fungal FPPS
genes.";
Curr. Genet. 30:232-239(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
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., 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.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
-!- 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.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
= diphosphate + (2E,6E)-farnesyl diphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
-!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate
biosynthesis; farnesyl diphosphate from geranyl diphosphate and
isopentenyl diphosphate: step 1/1.
-!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate
biosynthesis; geranyl diphosphate from dimethylallyl diphosphate
and isopentenyl diphosphate: step 1/1.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
{ECO:0000305}.
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EMBL; X96944; CAA65645.1; -; Genomic_DNA.
EMBL; AL670009; CAD21355.1; -; Genomic_DNA.
EMBL; CM002240; EAA32305.1; -; Genomic_DNA.
PIR; S71436; S71436.
RefSeq; XP_961541.1; XM_956448.2.
ProteinModelPortal; Q92250; -.
PRIDE; Q92250; -.
EnsemblFungi; EAA32305; EAA32305; NCU01175.
GeneID; 3877737; -.
KEGG; ncr:NCU01175; -.
EuPathDB; FungiDB:NCU01175; -.
HOGENOM; HOG000160912; -.
InParanoid; Q92250; -.
KO; K00787; -.
OMA; ITAPEDH; -.
OrthoDB; EOG092C35ZD; -.
UniPathway; UPA00259; UER00368.
UniPathway; UPA00260; UER00369.
Proteomes; UP000001805; Chromosome 2, Linkage Group V.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0004161; F:dimethylallyltranstransferase activity; IBA:GO_Central.
GO; GO:0004337; F:geranyltranstransferase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IBA:GO_Central.
GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.600.10; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR000092; Polyprenyl_synt.
InterPro; IPR033749; Polyprenyl_synt_CS.
Pfam; PF00348; polyprenyl_synt; 1.
SUPFAM; SSF48576; SSF48576; 1.
PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Isoprene biosynthesis;
Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
Reference proteome; Transferase.
CHAIN 1 347 Farnesyl pyrophosphate synthase.
/FTId=PRO_0000123950.
METAL 95 95 Magnesium 1. {ECO:0000250}.
METAL 95 95 Magnesium 2. {ECO:0000250}.
METAL 99 99 Magnesium 1. {ECO:0000250}.
METAL 99 99 Magnesium 2. {ECO:0000250}.
METAL 235 235 Magnesium 3. {ECO:0000250}.
BINDING 50 50 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 53 53 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 88 88 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 104 104 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 105 105 Isopentenyl diphosphate. {ECO:0000250}.
BINDING 192 192 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 193 193 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 232 232 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 249 249 Dimethylallyl diphosphate. {ECO:0000250}.
BINDING 258 258 Dimethylallyl diphosphate. {ECO:0000250}.
CONFLICT 134 134 L -> R (in Ref. 1; CAA65645).
{ECO:0000305}.
CONFLICT 321 321 I -> N (in Ref. 1; CAA65645).
{ECO:0000305}.
SEQUENCE 347 AA; 40278 MW; 83F4DC7C4D61212F CRC64;
MAKTTTLKEF ESVFPKLEEA LLEYAKAYKL PEQMLSWYKQ SLEVNTLGGK CNRGMSVPDS
ASILLGRPLT EEEYFQAATL GWMTELLQAF FLVSDDIMDS SITRRGKPCW YRQEGVGMVA
INDAFMLESA IYTLLKKYFR SHPRYVDFLE LFHEVTFQTE MGQLCDLLTA PEDKVDLDNF
SMDKYTFIVI YKTAYYSFYL PVALAMYMLD IATPENLKQA EDILIPLGEY FQVQDDYLDN
FGLPEHIGKI GTDIQDNKCS WLVNKALSIV TPEQRKTLEE NYGRKDKAKE AVIKQLYDDL
KLEDHYKQYE EERVGEIRKM IDAIDESKGL KKQVFEAFLG KIYKRSK


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