Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Geranylgeranyl pyrophosphate synthase paxG (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Paxilline synthesis protein G)

 PAXG_PENPX              Reviewed;         371 AA.
Q9C446;
11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 60.
RecName: Full=Geranylgeranyl pyrophosphate synthase paxG {ECO:0000250|UniProtKB:Q12051};
Short=GGPP synthase {ECO:0000305};
Short=GGPPSase {ECO:0000305};
EC=2.5.1.- {ECO:0000305};
AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
AltName: Full=Dimethylallyltranstransferase {ECO:0000250|UniProtKB:Q12051};
EC=2.5.1.1 {ECO:0000250|UniProtKB:Q12051};
AltName: Full=Farnesyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
AltName: Full=Farnesyltranstransferase {ECO:0000250|UniProtKB:Q12051};
EC=2.5.1.29 {ECO:0000250|UniProtKB:Q12051};
AltName: Full=Geranylgeranyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
AltName: Full=Geranyltranstransferase {ECO:0000250|UniProtKB:Q12051};
EC=2.5.1.10 {ECO:0000250|UniProtKB:Q12051};
AltName: Full=Paxilline synthesis protein G {ECO:0000303|PubMed:11169115};
Name=paxG {ECO:0000303|PubMed:11169115};
Penicillium paxilli.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
NCBI_TaxID=70109;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=PN2013;
PubMed=11169115; DOI=10.1046/j.1365-2958.2001.02265.x;
Young C., McMillan L., Telfer E., Scott B.;
"Molecular cloning and genetic analysis of an indole-diterpene gene
cluster from Penicillium paxilli.";
Mol. Microbiol. 39:754-764(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=PN2013;
PubMed=23949005; DOI=10.3390/toxins5081422;
Scott B., Young C.A., Saikia S., McMillan L.K., Monahan B.J.,
Koulman A., Astin J., Eaton C.J., Bryant A., Wrenn R.E., Finch S.C.,
Tapper B.A., Parker E.J., Jameson G.B.;
"Deletion and gene expression analyses define the paxilline
biosynthetic gene cluster in Penicillium paxilli.";
Toxins 5:1422-1446(2013).
[3]
FUNCTION.
PubMed=16494875; DOI=10.1016/j.febslet.2006.02.008;
Saikia S., Parker E.J., Koulman A., Scott B.;
"Four gene products are required for the fungal synthesis of the
indole-diterpene, paspaline.";
FEBS Lett. 580:1625-1630(2006).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND PEROXISOMAL TARGETING SIGNAL.
PubMed=19529962; DOI=10.1007/s00438-009-0463-5;
Saikia S., Scott B.;
"Functional analysis and subcellular localization of two
geranylgeranyl diphosphate synthases from Penicillium paxilli.";
Mol. Genet. Genomics 282:257-271(2009).
-!- FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene
cluster that mediates the biosynthesis of paxilline, a mycotoxin
that acts as an inhibitor of mammalian maxi-K channels
(PubMed:11169115, PubMed:23949005, PubMed:16494875,
PubMed:19529962). PaxG, the geranylgeranyl diphosphate (GGPP)
synthase is proposed to catalyze the first step in paxilline
biosynthesis (PubMed:23949005, PubMed:16494875, PubMed:19529962).
Condensation of indole-3-glycerol phosphate with GGPP by paxC then
forms 3-geranylgeranylindole (3-GGI), followed by epoxidation and
cyclization of this intermediate (by paxM and paxB) to form
paspaline (PubMed:23949005, PubMed:16494875). Paspaline is
subsequently converted to 13-desoxypaxilline by paxP, the latter
being then converted to paxilline by paxQ (PubMed:23949005).
Finally paxilline can be mono- and di-prenylated by paxD
(PubMed:23949005). {ECO:0000269|PubMed:11169115,
ECO:0000269|PubMed:16494875, ECO:0000269|PubMed:19529962,
ECO:0000269|PubMed:23949005}.
-!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl
diphosphate = diphosphate + geranyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate
= diphosphate + (2E,6E)-farnesyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + isopentenyl
diphosphate = diphosphate + geranylgeranyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q12051};
Note=Binds 3 Mg(2+) ions per subunit.
{ECO:0000250|UniProtKB:Q12051};
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:16494875, ECO:0000269|PubMed:19529962,
ECO:0000305|PubMed:11169115, ECO:0000305|PubMed:23949005}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19529962}.
-!- DISRUPTION PHENOTYPE: Impairs the production of paxilline
(PubMed:11169115, PubMed:23949005). {ECO:0000269|PubMed:11169115,
ECO:0000269|PubMed:23949005}.
-!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; HM171111; AAK11531.1; -; Genomic_DNA.
ProteinModelPortal; Q9C446; -.
SMR; Q9C446; -.
BioCyc; MetaCyc:MONOMER-18634; -.
GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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;
Isoprene biosynthesis; Magnesium; Metal-binding; Peroxisome;
Transferase.
CHAIN 1 371 Geranylgeranyl pyrophosphate synthase
paxG.
/FTId=PRO_0000436115.
MOTIF 369 371 Peroxisomal targeting signal.
{ECO:0000269|PubMed:19529962}.
METAL 128 128 Magnesium 1.
{ECO:0000250|UniProtKB:Q12051}.
METAL 128 128 Magnesium 2.
{ECO:0000250|UniProtKB:Q12051}.
METAL 132 132 Magnesium 1.
{ECO:0000250|UniProtKB:Q12051}.
METAL 132 132 Magnesium 2.
{ECO:0000250|UniProtKB:Q12051}.
METAL 252 252 Magnesium 3.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 89 89 Isopentenyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 92 92 Isopentenyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 121 121 Isopentenyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 137 137 Dimethylallyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 138 138 Isopentenyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 215 215 Dimethylallyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 216 216 Dimethylallyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 249 249 Dimethylallyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 256 256 Dimethylallyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 266 266 Dimethylallyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
BINDING 276 276 Dimethylallyl diphosphate.
{ECO:0000250|UniProtKB:Q12051}.
SITE 160 160 Important for determining product chain
length. {ECO:0000250|UniProtKB:Q12051}.
SEQUENCE 371 AA; 42352 MW; 6A006DA633EC5A61 CRC64;
MSYILAEALN FVRRGISHLN YWGASHSLSA DNYWESNFQG FPRLLSDSSK APSTIRTVQV
LEDDVDDIAI QYNKIVRGPL DYLLAIPGKD IRSKLIDSFN IWLQLPEEKL SIVKDIINLL
HTASLLIDDI QDASRLRRGK PVAHDVYGVA QTINSANYAY YLQQARLKEI GDPRAFEIFT
RSLLDLHLGQ GMDLYWRDMV VCPTEEEYTR MVMYKTGGLF NLALDLMRIQ SRKNTDFSKL
VELLGVIFQI RDDYMNLQSG LYAEKKGLME DLTEGKFSYP IIHSIRASPE SSELLDILKQ
RTEDEAVKIR AVKIMESTGS FQYTRETLSR LSAEARGYVK KLETSLGPNP GIHKILDLLE
VEYPTNEKGR V


Related products :

Catalog number Product name Quantity
30-424 GGPS1 is a member of the prenyltransferase family with geranylgeranyl diphosphate (GGPP) synthase activity. The enzyme catalyzes the synthesis of GGPP from farnesyl diphosphate and isopentenyl diphosp 0.05 mg
26-323 GGPS1 is a member of the prenyltransferase family and has geranylgeranyl diphosphate (GGPP) synthase activity. The enzyme catalyzes the synthesis of GGPP from farnesyl diphosphate and isopentenyl diph 0.05 mg
201-20-2023 FDPS{farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase)}rabbit.pAb 0.2ml
CSB-EL008563RA Rat farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Rat, Sample Type serum, plasma 96T
10-288-22413F Geranylgeranyl pyrophosphate synthetase - GGPP synthetase; GGPPSase; Geranylgeranyl diphosphate synthase 0.1 mg
10-288-22413F Geranylgeranyl pyrophosphate synthetase - GGPP synthetase; GGPPSase; Geranylgeranyl diphosphate synthase 0.05 mg
CSB-EL008563MO Mouse farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL008563HU Human farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL008563BO Bovine farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL008563CH Chicken farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) (FDPS) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-PA008563GA01HU Rabbit anti-human farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA008563GA01HU Rabbit anti-human farnesyl diphosphate synthase (farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
EIAAB11864 All-trans-decaprenyl-diphosphate synthase subunit 1,Decaprenyl pyrophosphate synthase subunit 1,Decaprenyl-diphosphate synthase subunit 1,Dps1,Mouse,Mus musculus,Pdss1,Solanesyl-diphosphate synthase s
EIAAB11424 All-trans-decaprenyl-diphosphate synthase subunit 2,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,Dlp1,Mouse,Mus musculus,Pdss2,Solanesyl-diphosphate synthase s
EIAAB11423 All-trans-decaprenyl-diphosphate synthase subunit 2,C6orf210,Candidate tumor suppressor protein,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,DLP1,Homo sapiens,
CD08 Human Geranylgeranyl Pyrophosphate Synthase GGPP Synthase l0
C227 Human Geranylgeranyl Pyrophosphate Synthase GGPP Synthase 50
C229 Geranylgeranyl Pyrophosphate Synthase GGPP Synthase lmg
C229 Geranylgeranyl Pyrophosphate Synthase GGPP Synthase 500
EIAAB11422 All-trans-decaprenyl-diphosphate synthase subunit 2,Decaprenyl pyrophosphate synthase subunit 2,Decaprenyl-diphosphate synthase subunit 2,Dlp1,Pdss2,Rat,Rattus norvegicus
EIAAB11863 All-trans-decaprenyl-diphosphate synthase subunit 1,Decaprenyl pyrophosphate synthase subunit 1,Decaprenyl-diphosphate synthase subunit 1,DPS1,Homo sapiens,Human,PDSS1,TPRT,TPT 1,Trans-prenyltransfera
orb90108 Human Geranylgeranyl Diphosphate Synthase 1 protein Enzymes 5
enz-555 Recombinant Human Geranylgeranyl Diphosphate Synthase 1 20
enz-555 Recombinant Human Geranylgeranyl Diphosphate Synthase 1 1mg
REN-555 Recombinant Human Geranylgeranyl Diphosphate Synthase 1 5


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur