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

Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.19) (Protein glycosylation B)

 PGLB_CAMJR              Reviewed;         713 AA.
Q5HTX9;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
05-DEC-2018, entry version 67.
RecName: Full=Undecaprenyl-diphosphooligosaccharide--protein glycotransferase;
EC=2.4.99.19 {ECO:0000269|PubMed:20007322};
AltName: Full=Protein glycosylation B;
Name=pglB; OrderedLocusNames=CJE1268;
Campylobacter jejuni (strain RM1221).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=195099;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RM1221;
PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
Nelson K.E.;
"Major structural differences and novel potential virulence mechanisms
from the genomes of multiple Campylobacter species.";
PLoS Biol. 3:72-85(2005).
[2]
DOMAIN.
PubMed=21812456; DOI=10.1021/bi201018d;
Jaffee M.B., Imperiali B.;
"Exploiting topological constraints to reveal buried sequence motifs
in the membrane-bound N-linked oligosaccharyl transferases.";
Biochemistry 50:7557-7567(2011).
[3]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 428-713, FUNCTION, AND
MUTAGENESIS OF SER-52; ASN-53; ASP-54; MET-568; SER-569; LEU-570 AND
ILE-571.
STRAIN=RM1221;
PubMed=20007322; DOI=10.1074/jbc.M109.081752;
Maita N., Nyirenda J., Igura M., Kamishikiryo J., Kohda D.;
"Comparative structural biology of eubacterial and archaeal
oligosaccharyltransferases.";
J. Biol. Chem. 285:4941-4950(2010).
-!- FUNCTION: Oligosaccharyltransferase that catalyzes the transfer of
a preassembled heptasaccharide from a lipid donor to an asparagine
residue in nascent polypeptide chains, affording a beta-linked
glycan to the asparagine side chain of target proteins.
{ECO:0000269|PubMed:20007322}.
-!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the
initial transfer of a defined glycan
(GalNAc(2)GlcGalNAc(3)Bac(NAc)(2) in eubacteria, where Bac(NAc)(2)
is di-N-acetyl bacillosamine) from the lipid carrier undecaprenol-
pyrophosphate to an asparagine residue within an Asp/Glu-Asn-X-
Ser/Thr consensus motif in nascent polypeptide chains, the first
step in protein N-glycosylation. {ECO:0000250|UniProtKB:B9KDD4}.
-!- CATALYTIC ACTIVITY:
Reaction=Tritrans,heptacis-undecaprenyl diphosphooligosaccharide +
[protein]-L-asparagine = tritrans,heptacis-undecaprenyl
diphosphate + a glycoprotein with the oligosaccharide chain
attached by N-beta-D-glycosyl linkage to protein L-asparagine.;
EC=2.4.99.19; Evidence={ECO:0000269|PubMed:20007322};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:B9KDD4};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:B9KDD4};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000250|UniProtKB:B9KDD4}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000250|UniProtKB:B9KDD4}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:B9KDD4}.
-!- DOMAIN: Despite low primary sequence conservation between
eukaryotic catalytic subunits and bacterial and archaeal single
subunit OSTs (ssOST), structural comparison revealed several
common motifs at spatially equivalent positions, like the DXD
motif 1 on the external loop 1 and the DXD motif 2 on the external
loop 2 involved in binding of the metal ion cofactor and the
carboxamide group of the acceptor asparagine, the conserved Glu
residue of the TIXE/SVSE motif on the external loop 5 involved in
catalysis, as well as the WWDYG and the DK/MI motifs in the
globular domain that define the binding pocket for the +2 Ser/Thr
of the acceptor sequon. In bacterial ssOSTs, an Arg residue was
found to interact with a negatively charged side chain at the -2
position of the sequon. This Arg is conserved in bacterial enzymes
and correlates with an extended sequon requirement (Asp-X-Asn-X-
Ser/Thr) for bacterial N-glycosylation.
{ECO:0000250|UniProtKB:B9KDD4}.
-!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; CP000025; AAW35590.1; -; Genomic_DNA.
RefSeq; WP_011049884.1; NC_003912.7.
PDB; 3AAG; X-ray; 2.80 A; A/B=428-713.
PDBsum; 3AAG; -.
SMR; Q5HTX9; -.
CAZy; GT66; Glycosyltransferase Family 66.
EnsemblBacteria; AAW35590; AAW35590; CJE1268.
KEGG; cjr:CJE1268; -.
HOGENOM; HOG000103852; -.
KO; K17251; -.
OMA; GYPIRYY; -.
BioCyc; CJEJ195099:G1G43-1269-MONOMER; -.
BRENDA; 2.4.99.18; 1087.
BRENDA; 2.4.99.19; 1087.
UniPathway; UPA00378; -.
EvolutionaryTrace; Q5HTX9; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IMP:TIGR.
GO; GO:0006487; P:protein N-linked glycosylation; IMP:TIGR.
InterPro; IPR003674; Oligo_trans_STT3.
Pfam; PF02516; STT3; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Glycoprotein;
Glycosyltransferase; Magnesium; Membrane; Metal-binding; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 713 Undecaprenyl-diphosphooligosaccharide--
protein glycotransferase.
/FTId=PRO_0000422588.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000305}.
TRANSMEM 12 35 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 36 96 Periplasmic. {ECO:0000305}.
TRANSMEM 97 122 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 123 125 Cytoplasmic. {ECO:0000305}.
TRANSMEM 126 144 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 145 152 Periplasmic. {ECO:0000305}.
TRANSMEM 153 174 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 175 176 Cytoplasmic. {ECO:0000305}.
TRANSMEM 177 192 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 193 197 Periplasmic. {ECO:0000305}.
TRANSMEM 198 215 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 216 220 Cytoplasmic. {ECO:0000305}.
TRANSMEM 221 233 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 234 237 Periplasmic. {ECO:0000305}.
TRANSMEM 238 254 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 255 260 Cytoplasmic. {ECO:0000305}.
TRANSMEM 261 278 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 279 324 Periplasmic. {ECO:0000305}.
TRANSMEM 325 347 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 348 352 Cytoplasmic. {ECO:0000305}.
TRANSMEM 353 369 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 370 373 Periplasmic. {ECO:0000305}.
TRANSMEM 374 396 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 397 406 Cytoplasmic. {ECO:0000305}.
TRANSMEM 407 427 Helical. {ECO:0000250|UniProtKB:B9KDD4}.
TOPO_DOM 428 713 Periplasmic. {ECO:0000305}.
REGION 194 196 Lipid-linked oligosaccharide binding.
{ECO:0000250|UniProtKB:B9KDD4}.
REGION 457 459 Target acceptor peptide binding.
{ECO:0000250|UniProtKB:B9KDD4}.
MOTIF 52 54 DXD motif 1.
{ECO:0000305|PubMed:21812456}.
MOTIF 152 154 DXD motif 2.
{ECO:0000305|PubMed:21812456}.
MOTIF 313 316 TIXE motif.
{ECO:0000305|PubMed:21812456}.
MOTIF 457 461 WWDYG motif.
{ECO:0000305|PubMed:21812456}.
MOTIF 568 575 MI motif. {ECO:0000250|UniProtKB:O29918}.
METAL 54 54 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
METAL 152 152 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
METAL 316 316 Manganese.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 54 54 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 291 291 Lipid-linked oligosaccharide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 316 316 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 328 328 Target acceptor peptide; important for
extended sequon recognition.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 372 372 Lipid-linked oligosaccharide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 462 462 Lipid-linked oligosaccharide.
{ECO:0000250|UniProtKB:B9KDD4}.
BINDING 571 571 Target acceptor peptide.
{ECO:0000250|UniProtKB:B9KDD4}.
SITE 145 145 Important for catalytic activity.
{ECO:0000250|UniProtKB:B9KDD4}.
CARBOHYD 534 534 N-linked (DATDGlc) asparagine.
{ECO:0000250|UniProtKB:B9KDD4}.
MUTAGEN 52 52 S->E,D: Strongly reduced catalytic
activity. {ECO:0000269|PubMed:20007322}.
MUTAGEN 53 53 N->A: Reduced catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 54 54 D->A: Strongly reduced catalytic
activity. {ECO:0000269|PubMed:20007322}.
MUTAGEN 568 568 M->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 569 569 S->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 570 570 L->A: No effect on catalytic activity.
{ECO:0000269|PubMed:20007322}.
MUTAGEN 571 571 I->A: Strong reduction in catalytic
activity. {ECO:0000269|PubMed:20007322}.
HELIX 437 444 {ECO:0000244|PDB:3AAG}.
STRAND 453 455 {ECO:0000244|PDB:3AAG}.
HELIX 458 460 {ECO:0000244|PDB:3AAG}.
HELIX 461 468 {ECO:0000244|PDB:3AAG}.
HELIX 481 492 {ECO:0000244|PDB:3AAG}.
HELIX 495 510 {ECO:0000244|PDB:3AAG}.
HELIX 525 531 {ECO:0000244|PDB:3AAG}.
TURN 532 534 {ECO:0000244|PDB:3AAG}.
HELIX 538 544 {ECO:0000244|PDB:3AAG}.
STRAND 560 565 {ECO:0000244|PDB:3AAG}.
HELIX 566 570 {ECO:0000244|PDB:3AAG}.
HELIX 572 577 {ECO:0000244|PDB:3AAG}.
STRAND 594 597 {ECO:0000244|PDB:3AAG}.
STRAND 599 601 {ECO:0000244|PDB:3AAG}.
STRAND 606 609 {ECO:0000244|PDB:3AAG}.
STRAND 614 616 {ECO:0000244|PDB:3AAG}.
TURN 624 626 {ECO:0000244|PDB:3AAG}.
STRAND 632 639 {ECO:0000244|PDB:3AAG}.
STRAND 644 649 {ECO:0000244|PDB:3AAG}.
STRAND 657 660 {ECO:0000244|PDB:3AAG}.
STRAND 670 674 {ECO:0000244|PDB:3AAG}.
TURN 678 680 {ECO:0000244|PDB:3AAG}.
HELIX 682 686 {ECO:0000244|PDB:3AAG}.
STRAND 697 699 {ECO:0000244|PDB:3AAG}.
STRAND 704 712 {ECO:0000244|PDB:3AAG}.
SEQUENCE 713 AA; 82206 MW; B5D4836BF36D8FF8 CRC64;
MLKKEYLKNP YLVLFAMIIL AYVFSVLCRF YWIWWASEFN EYFFNNQLMI ISNDGYAFAE
GARDMIAGFH QPNDLSYYGS SLSTLTYWLY KITPFSFESI ILYMSTFLSS LVVIPIILLA
NEYKRPLMGF VAALLASVAN SYYNRTMSGY YDTDMLVIVL PMFILFFMVR MILKKDFFSL
IALPLFIGIY LWWYPSSYTL NVALIGLFLI YTLIFHRKEK IFYIAVILSS LTLSNIAWFY
QSAIIVILFA LFALEQKRLN FMIIGILGSA TLIFLILSGG VDPILYQLKF YIFRNDESAN
LTQGFMYFNV NQTIQEVENV DFSEFMRRIS GSEIVFLFSL FGFVWLLRKH KSMIMALPIL
VLGFLALKGG LRFTIYSVPV MALGFGFLLS EFKAILVKKY SQLTSNVCIV FATILTLAPV
FIHIYNYKAP TVFSQNEASL LNQLKNIANR EDYVVTWWDY GYPVRYYSDV KTLVDGGKHL
GKDNFFPSFA LSKDEQAAAN MARLSVEYTE KSFYAPQNDI LKSDILQAMM KDYNQSNVDL
FLASLSKPDF KIDTPKTRDI YLYMPARMSL IFSTVASFSF INLDTGVLDK PFTFSTAYPL
DVKNGEIYLS NGVVLSDDFR SFKIGDNVVS VNSIVEINSI KQGEYKITPI DDKAQFYIFY
LKDSAIPYAQ FILMDKTMFN SAYVQMFFLG NYDKNLFDLV INSRDAKVFK LKI


Related products :

Catalog number Product name Quantity
EIAAB35895 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2,Homo sapiens,Human,RIBIIR,Ribophorin II,Ribophori
EIAAB35893 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1,Homo sapiens,Human,Ribophorin I,Ribophorin-1,RPN1
EIAAB35899 Bos taurus,Bovine,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2,Ribophorin II,Ribophorin-2,RPN2
EIAAB35891 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1,Mouse,Mus musculus,Ribophorin I,Ribophorin-1,Rpn1
EIAAB35892 Chicken,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 65 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1,Gallus gallus,Oligosaccharyl transferase
EIAAB35894 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1,Rat,Rattus norvegicus,Ribophorin I,Ribophorin-1,R
EIAAB35898 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2,Mouse,Mus musculus,Ribophorin II,Ribophorin-2,Rpn
EIAAB35890 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1,Pig,Ribophorin I,Ribophorin-1,RPN1,RPN-I,Sus scro
EIAAB35897 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2,Rat,Rattus norvegicus,Ribophorin II,Ribophorin-2,
PE051244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit protein 1mg
PE051244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit protein 5mg
PE051244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit protein 200ug
PE051244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit protein 50ug
PE031244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein 5mg
PE031244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein 200ug
PE031244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein 1mg
PE031244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein 50ug
15-5117 Antigens Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein, Human, Recombinant, E.coli 20
EIAAB35900 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 63 kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2,Pig,Ribophorin II,Ribophorin-2,RPN2,RPN-II,Sus sc
CSB-RP031244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein, Mol. Weight 13 KD, Source E.coli derived 50ug
CSB-RP031244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein, Mol. Weight 13 KD, Source E.coli derived 200ug
CSB-RP031244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein, Mol. Weight 13 KD, Source E.coli derived 1mg
CSB-RP031244h Recombinant human Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 protein, Mol. Weight 13 KD, Source E.coli derived 10ug
EIAAB35896 Chicken,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 65-II kDa subunit,Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2,Gallus gallus,Ribophorin II,Ribophorin
DDR2 DDOST Gene dolichyl-diphosphooligosaccharide--protein glycosyltransferase


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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