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

mRNA cap guanine-N7 methyltransferase (EC 2.1.1.56) (mRNA (guanine-N(7)-)-methyltransferase) (mRNA cap methyltransferase)

 MCES_ENCCU              Reviewed;         283 AA.
Q8SR66;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 2.
30-AUG-2017, entry version 85.
RecName: Full=mRNA cap guanine-N7 methyltransferase;
EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
AltName: Full=mRNA (guanine-N(7)-)-methyltransferase;
AltName: Full=mRNA cap methyltransferase;
Name=ABD1; OrderedLocusNames=ECU10_0380;
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
Eukaryota; Fungi; Microsporidia; Unikaryonidae; Encephalitozoon.
NCBI_TaxID=284813;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GB-M1;
PubMed=11719806; DOI=10.1038/35106579;
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M.,
Weissenbach J., Vivares C.P.;
"Genome sequence and gene compaction of the eukaryote parasite
Encephalitozoon cuniculi.";
Nature 414:450-453(2001).
[2]
GENOME REANNOTATION.
STRAIN=GB-M1;
PubMed=20003517; DOI=10.1186/1471-2164-10-607;
Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
Cornman R.S., Evans J.D., Delbac F., Peyret P.;
"Identification of transcriptional signals in Encephalitozoon cuniculi
widespread among Microsporidia phylum: support for accurate structural
genome annotation.";
BMC Genomics 10:607-607(2009).
[3]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES,
AND MUTAGENESIS OF ARG-32; ASN-35; ASN-36; LYS-39; LYS-60; ASP-63;
LYS-66; ASP-79; ILE-80; ARG-91; 107-ASP-SER-108; TYR-109; PHE-126;
LEU-201 AND TYR-269.
PubMed=14731396; DOI=10.1016/S1097-2765(03)00522-7;
Fabrega C., Hausmann S., Shen V., Shuman S., Lima C.D.;
"Structure and mechanism of mRNA cap (guanine-N7) methyltransferase.";
Mol. Cell 13:77-89(2004).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF LYS-39; ASP-55; ASP-63 AND ASP-79.
PubMed=15760890; DOI=10.1074/jbc.M501073200;
Hausmann S., Zheng S., Fabrega C., Schneller S.W., Lima C.D.,
Shuman S.;
"Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase:
methyl acceptor specificity, inhibition by S-adenosylmethionine
analogs, and structure-guided mutational analysis.";
J. Biol. Chem. 280:20404-20412(2005).
[5]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG, AND MUTAGENESIS OF ASN-36; LYS-39; ASP-55; LYS-60; ASP-63;
LYS-66; ASP-79; ARG-91; TYR-109; PHE-126; HIS-129; TYR-130 AND
GLU-210.
PubMed=16971388; DOI=10.1074/jbc.M607292200;
Zheng S., Hausmann S., Liu Q., Ghosh A., Schwer B., Lima C.D.,
Shuman S.;
"Mutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7)
methyltransferase, structure of the enzyme bound to sinefungin, and
evidence that cap methyltransferase is the target of sinefungin's
antifungal activity.";
J. Biol. Chem. 281:35904-35913(2006).
-!- FUNCTION: mRNA-capping methyltransferase that methylates the N7
position of the added guanosine to the 5'-cap structure of mRNAs.
Binds RNA containing 5'-terminal GpppC.
{ECO:0000269|PubMed:15760890}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-
ProRule:PRU00895}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1 mM for GTP {ECO:0000269|PubMed:15760890};
KM=25 uM for S-adenosyl-L-methionine
{ECO:0000269|PubMed:15760890};
KM=0.1 mM for cap dinucleotide GpppA
{ECO:0000269|PubMed:15760890};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15760890,
ECO:0000269|PubMed:16971388}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. mRNA cap 0 methyltransferase
family. {ECO:0000255|PROSITE-ProRule:PRU00895}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL590449; CAD25757.2; -; Genomic_DNA.
RefSeq; NP_586153.1; NM_001041986.1.
PDB; 1RI1; X-ray; 2.50 A; A=1-283.
PDB; 1RI2; X-ray; 2.70 A; A=1-283.
PDB; 1RI3; X-ray; 2.50 A; A=1-283.
PDB; 1RI4; X-ray; 2.40 A; A=1-283.
PDB; 1RI5; X-ray; 2.10 A; A=1-283.
PDB; 1Z3C; X-ray; 2.20 A; A=1-283.
PDB; 2HV9; X-ray; 2.60 A; A=1-283.
PDBsum; 1RI1; -.
PDBsum; 1RI2; -.
PDBsum; 1RI3; -.
PDBsum; 1RI4; -.
PDBsum; 1RI5; -.
PDBsum; 1Z3C; -.
PDBsum; 2HV9; -.
ProteinModelPortal; Q8SR66; -.
SMR; Q8SR66; -.
STRING; 284813.NP_586153.1; -.
EnsemblFungi; CAD25757; CAD25757; CAD25757.
GeneID; 859802; -.
KEGG; ecu:ECU10_0380; -.
EuPathDB; MicrosporidiaDB:ECU10_0380; -.
eggNOG; KOG1975; Eukaryota.
eggNOG; ENOG410Y7HG; LUCA.
HOGENOM; HOG000242614; -.
InParanoid; Q8SR66; -.
KO; K00565; -.
OrthoDB; EOG092C2SMS; -.
BRENDA; 2.1.1.56; 7412.
EvolutionaryTrace; Q8SR66; -.
Proteomes; UP000000819; Chromosome X.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
InterPro; IPR016899; mRNA_G-N7_MeTrfase.
InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF03291; Pox_MCEL; 1.
PIRSF; PIRSF028762; ABD1; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51562; RNA_CAP0_MT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Methyltransferase; mRNA capping;
mRNA processing; Nucleus; Reference proteome; RNA-binding;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 283 mRNA cap guanine-N7 methyltransferase.
/FTId=PRO_0000210142.
DOMAIN 1 283 mRNA cap 0 methyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
REGION 35 36 mRNA cap binding.
BINDING 39 39 S-adenosyl-L-methionine.
BINDING 57 57 S-adenosyl-L-methionine; via carbonyl
oxygen.
BINDING 79 79 S-adenosyl-L-methionine.
BINDING 107 107 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000250|UniProtKB:O43148}.
BINDING 125 125 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:O43148}.
BINDING 129 129 mRNA cap.
BINDING 130 130 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:O43148}.
BINDING 210 210 mRNA cap.
BINDING 269 269 mRNA cap.
SITE 60 60 mRNA cap binding.
SITE 66 66 mRNA cap binding.
SITE 91 91 mRNA cap binding.
MUTAGEN 32 32 R->A: No effect. Loss of activity; when
associated with A-60.
{ECO:0000269|PubMed:14731396}.
MUTAGEN 35 35 N->A: No effect. Loss of activity; when
associated with A-269.
{ECO:0000269|PubMed:14731396}.
MUTAGEN 36 36 N->A: Reduces activity by 85%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 36 36 N->D: Reduces activity by 96%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 39 39 K->A,Q,R: Loss of activity.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:15760890,
ECO:0000269|PubMed:16971388}.
MUTAGEN 55 55 D->A,N: Reduces activity by 95%.
{ECO:0000269|PubMed:15760890,
ECO:0000269|PubMed:16971388}.
MUTAGEN 55 55 D->E: Reduces activity by 60%.
{ECO:0000269|PubMed:15760890,
ECO:0000269|PubMed:16971388}.
MUTAGEN 60 60 K->A: Reduces activity by 92%. Loss of
activity; when associated with A-32.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 63 63 D->A,N: Reduces activity by 99%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:15760890,
ECO:0000269|PubMed:16971388}.
MUTAGEN 63 63 D->E: Reduces activity by 75%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:15760890,
ECO:0000269|PubMed:16971388}.
MUTAGEN 66 66 K->A: Reduces activity by 80%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 66 66 K->Q,R: Reduces activity by 90%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 79 79 D->A,N: Loss of activity.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:15760890,
ECO:0000269|PubMed:16971388}.
MUTAGEN 79 79 D->E: Reduces activity by 77%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:15760890,
ECO:0000269|PubMed:16971388}.
MUTAGEN 80 80 I->A: No effect. Strongly reduced
activity; when associated with A-109.
{ECO:0000269|PubMed:14731396}.
MUTAGEN 91 91 R->A,Q: Reduces activity by over 98%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 91 91 R->K: Reduces activity by 96%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 107 108 DS->AA: Slightly reduced activity.
{ECO:0000269|PubMed:14731396}.
MUTAGEN 109 109 Y->A: Reduces activity by 83%. Strongly
reduced activity; when associated with A-
80. {ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 126 126 F->A,N: Loss of activity.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 126 126 F->H: Reduces activity by 92%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 126 126 F->I: Reduces activity by 75%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 126 126 F->L: Reduces activity by 55%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 126 126 F->V: Reduces activity by 84%.
{ECO:0000269|PubMed:14731396,
ECO:0000269|PubMed:16971388}.
MUTAGEN 129 129 H->A: Reduces activity by 53%. Reduces
activity by 99%; when associated with L-
130. {ECO:0000269|PubMed:16971388}.
MUTAGEN 130 130 Y->A,S,V: Reduces activity by 98%.
{ECO:0000269|PubMed:16971388}.
MUTAGEN 130 130 Y->F: Reduces activity by 66%.
{ECO:0000269|PubMed:16971388}.
MUTAGEN 130 130 Y->L: Reduces activity by 99%; when
associated with A-129.
{ECO:0000269|PubMed:16971388}.
MUTAGEN 201 201 L->A: No effect.
{ECO:0000269|PubMed:14731396}.
MUTAGEN 210 210 E->A: Reduces activity by 87%.
{ECO:0000269|PubMed:16971388}.
MUTAGEN 269 269 Y->A: Reduced activity. Loss of activity;
when associated with A-35.
{ECO:0000269|PubMed:14731396}.
HELIX 29 46 {ECO:0000244|PDB:1RI5}.
STRAND 52 56 {ECO:0000244|PDB:1RI5}.
TURN 59 63 {ECO:0000244|PDB:1RI5}.
HELIX 64 70 {ECO:0000244|PDB:1RI5}.
STRAND 73 80 {ECO:0000244|PDB:1RI5}.
HELIX 82 93 {ECO:0000244|PDB:1RI5}.
STRAND 98 106 {ECO:0000244|PDB:1RI5}.
TURN 108 110 {ECO:0000244|PDB:1RI5}.
STRAND 119 126 {ECO:0000244|PDB:1RI5}.
HELIX 128 132 {ECO:0000244|PDB:1RI5}.
HELIX 135 147 {ECO:0000244|PDB:1RI5}.
STRAND 149 160 {ECO:0000244|PDB:1RI5}.
HELIX 162 171 {ECO:0000244|PDB:1RI5}.
STRAND 177 182 {ECO:0000244|PDB:1RI5}.
TURN 191 193 {ECO:0000244|PDB:1RI5}.
STRAND 196 201 {ECO:0000244|PDB:1RI5}.
STRAND 206 211 {ECO:0000244|PDB:1RI5}.
HELIX 215 223 {ECO:0000244|PDB:1RI5}.
TURN 224 226 {ECO:0000244|PDB:1RI5}.
STRAND 227 234 {ECO:0000244|PDB:1RI5}.
HELIX 235 244 {ECO:0000244|PDB:1RI5}.
HELIX 247 251 {ECO:0000244|PDB:1RI5}.
STRAND 252 254 {ECO:0000244|PDB:1RI5}.
HELIX 260 266 {ECO:0000244|PDB:1RI5}.
STRAND 269 276 {ECO:0000244|PDB:1RI5}.
SEQUENCE 283 AA; 33074 MW; 40ABA7B1522C7001 CRC64;
MEGKKEEIRE HYNSIRERGR ESRQRSKTIN IRNANNFIKA CLIRLYTKRG DSVLDLGCGK
GGDLLKYERA GIGEYYGVDI AEVSINDARV RARNMKRRFK VFFRAQDSYG RHMDLGKEFD
VISSQFSFHY AFSTSESLDI AQRNIARHLR PGGYFIMTVP SRDVILERYK QGRMSNDFYK
IELEKMEDVP MESVREYRFT LLDSVNNCIE YFVDFTRMVD GFKRLGLSLV ERKGFIDFYE
DEGRRNPELS KKMGLGCLTR EESEVVGIYE VVVFRKLVPE SDA


Related products :

Catalog number Product name Quantity
25-621 RNMT belongs to the mRNA cap methyltransferase family. RNMT is a mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. It binds RNA co 0.05 mg
CSB-EL019902RA Rat mRNA cap guanine-N7 methyltransferase(RNMT) ELISA kit 96T
CSB-EL019902MO Mouse mRNA cap guanine-N7 methyltransferase(RNMT) ELISA kit 96T
CSB-EL019902HU Human mRNA cap guanine-N7 methyltransferase(RNMT) ELISA kit 96T
CSB-EL019902RA Rat mRNA cap guanine-N7 methyltransferase(RNMT) ELISA kit SpeciesRat 96T
CSB-EL019902MO Mouse mRNA cap guanine-N7 methyltransferase(RNMT) ELISA kit SpeciesMouse 96T
CSB-EL019902HU Human mRNA cap guanine-N7 methyltransferase(RNMT) ELISA kit SpeciesHuman 96T
EIAAB25760 Bos taurus,Bovine,Cap1 2'O-ribose methyltransferase 1,Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1,FtsJ methyltransferase domain-containing protein 2,FTSJD2,MTr1
EIAAB25757 Cap1 2'O-ribose methyltransferase 1,Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1,FtsJ methyltransferase domain-containing protein 2,Ftsjd2,MTr1,Rat,Rattus norvegicus
EIAAB25759 Cap1 2'O-ribose methyltransferase 1,Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1,FtsJ methyltransferase domain-containing protein 2,Ftsjd2,Kiaa0082,Mouse,MTr1,Mus musculus
MCES_MOUSE ELISA Kit FOR mRNA cap guanine-N7 methyltransferase; organism: Mouse; gene name: Rnmt 96T
EIAAB25758 Cap1 2'O-ribose methyltransferase 1,Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1,FtsJ methyltransferase domain-containing protein 2,FTSJD2,hMTr1,Homo sapiens,Human,Interferon-stimulated ge
26-565 DCP1B may play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It may remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5' 0.05 mg
EIAAB44050 Homo sapiens,Human,KIAA1393,M1G-methyltransferase,TRM5,TRMT5,tRNA (guanine-N(1)-)-methyltransferase,tRNA [GM37] methyltransferase,tRNA methyltransferase 5
29-510 DCP2 is necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. DCP2 removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-pho 0.05 mg
EIAAB44052 Kiaa1393,M1G-methyltransferase,Mouse,Mus musculus,Trmt5,tRNA (guanine-N(1)-)-methyltransferase,tRNA [GM37] methyltransferase,tRNA methyltransferase 5
EIAAB44051 Bos taurus,Bovine,M1G-methyltransferase,TRMT5,tRNA (guanine-N(1)-)-methyltransferase,tRNA [GM37] methyltransferase,tRNA methyltransferase 5
EIAAB44047 C12orf1,Homo sapiens,Human,Methyltransferase-like protein 1,METTL1,tRNA (guanine-N(7)-)-methyltransferase,tRNA(m7G46)-methyltransferase
EIAAB44046 Methyltransferase-like protein 1,Mettl1,Mouse,Mus musculus,tRNA (guanine-N(7)-)-methyltransferase,tRNA(m7G46)-methyltransferase
EIAAB44045 Bos taurus,Bovine,Methyltransferase-like protein 1,METTL1,tRNA (guanine-N(7)-)-methyltransferase,tRNA(m7G46)-methyltransferase
E2223Rb Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus,Rabbit
E2223h Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT
U2223Rb CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus, 96T
E2223Rb ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus 96T
U2223m CLIA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Tem 96T


 

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