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

Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)]

 GLMU_YERPE              Reviewed;         456 AA.
Q8Z9S7; Q0W9R8; Q74PA2; Q8CZF5;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
22-NOV-2017, entry version 104.
RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631};
Includes:
RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631};
EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631};
AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
Includes:
RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631};
Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631};
OrderedLocusNames=YPO4119, y4133, YP_4026;
Yersinia pestis.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Yersiniaceae; Yersinia.
NCBI_TaxID=632;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CO-92 / Biovar Orientalis;
PubMed=11586360; DOI=10.1038/35097083;
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G.,
Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V.,
Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M.,
Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
"Genome sequence of Yersinia pestis, the causative agent of plague.";
Nature 413:523-527(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KIM10+ / Biovar Mediaevalis;
PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C.,
Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V.,
Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R.,
Perry R.D.;
"Genome sequence of Yersinia pestis KIM.";
J. Bacteriol. 184:4601-4611(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=91001 / Biovar Mediaevalis;
PubMed=15368893; DOI=10.1093/dnares/11.3.179;
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z.,
Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J.,
Yang H., Wang J., Huang P., Yang R.;
"Complete genome sequence of Yersinia pestis strain 91001, an isolate
avirulent to humans.";
DNA Res. 11:179-197(2004).
[4]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC
ANALOG.
Nocek B., Kuhn M., Gu M., Anderson W.F., Joachimiak A.;
"Crystal structure of yersinia pestis GlmU in comlex with alp
glucosamine 1-phosphate (gp1).";
Submitted (MAY-2012) to the PDB data bank.
-!- FUNCTION: Catalyzes the last two sequential reactions in the de
novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-
GlcNAc). The C-terminal domain catalyzes the transfer of acetyl
group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P)
to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is
converted into UDP-GlcNAc by the transfer of uridine 5-
monophosphate (from uridine 5-triphosphate), a reaction catalyzed
by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate =
CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.
{ECO:0000255|HAMAP-Rule:MF_01631}.
-!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
= diphosphate + UDP-N-acetyl-alpha-D-glucosamine.
{ECO:0000255|HAMAP-Rule:MF_01631}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250, ECO:0000255|HAMAP-Rule:MF_01631};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250,
ECO:0000255|HAMAP-Rule:MF_01631};
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate
from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
{ECO:0000255|HAMAP-Rule:MF_01631}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_01631}.
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A
biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01631}.
-!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01631}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
-!- SIMILARITY: In the N-terminal section; belongs to the N-
acetylglucosamine-1-phosphate uridyltransferase family.
{ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the transferase
hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631,
ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM87675.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAS64165.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL590842; CAL22687.1; -; Genomic_DNA.
EMBL; AE009952; AAM87675.1; ALT_INIT; Genomic_DNA.
EMBL; AE017042; AAS64165.1; ALT_INIT; Genomic_DNA.
PIR; AC0500; AC0500.
RefSeq; WP_002215550.1; NZ_LT605018.1.
RefSeq; YP_002348970.1; NC_003143.1.
PDB; 4FCE; X-ray; 1.96 A; A=1-456.
PDBsum; 4FCE; -.
ProteinModelPortal; Q8Z9S7; -.
SMR; Q8Z9S7; -.
IntAct; Q8Z9S7; 6.
STRING; 187410.y4133; -.
PRIDE; Q8Z9S7; -.
DNASU; 1149080; -.
EnsemblBacteria; AAM87675; AAM87675; y4133.
EnsemblBacteria; AAS64165; AAS64165; YP_4026.
GeneID; 1176947; -.
KEGG; ype:YPO4119; -.
KEGG; ypj:CH55_2801; -.
KEGG; ypk:y4133; -.
KEGG; ypl:CH46_929; -.
KEGG; ypm:YP_4026; -.
KEGG; ypv:BZ15_3583; -.
KEGG; ypw:CH59_2076; -.
PATRIC; fig|214092.21.peg.4663; -.
eggNOG; ENOG4105CAJ; Bacteria.
eggNOG; COG1207; LUCA.
HOGENOM; HOG000283476; -.
KO; K04042; -.
UniPathway; UPA00113; UER00532.
UniPathway; UPA00113; UER00533.
UniPathway; UPA00973; -.
Proteomes; UP000000815; Chromosome.
Proteomes; UP000001019; Chromosome.
Proteomes; UP000002490; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_01631; GlmU; 1.
InterPro; IPR005882; Bifunctional_GlmU.
InterPro; IPR001451; Hexapep.
InterPro; IPR018357; Hexapep_transf_CS.
InterPro; IPR025877; MobA-like_NTP_Trfase.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR011004; Trimer_LpxA-like_sf.
Pfam; PF00132; Hexapep; 3.
Pfam; PF12804; NTP_transf_3; 1.
SUPFAM; SSF51161; SSF51161; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR01173; glmU; 1.
PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Cell shape;
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
Magnesium; Metal-binding; Multifunctional enzyme;
Nucleotidyltransferase; Peptidoglycan synthesis; Reference proteome;
Repeat; Transferase.
CHAIN 1 456 Bifunctional protein GlmU.
/FTId=PRO_0000233888.
REGION 1 229 Pyrophosphorylase. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 11 14 UDP-GlcNAc binding. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 81 82 UDP-GlcNAc binding. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 103 105 UDP-GlcNAc binding. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 230 250 Linker. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 251 456 N-acetyltransferase. {ECO:0000255|HAMAP-
Rule:MF_01631}.
REGION 386 387 Acetyl-CoA binding. {ECO:0000255|HAMAP-
Rule:MF_01631}.
ACT_SITE 363 363 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01631}.
METAL 105 105 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01631}.
METAL 227 227 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 25 25 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 76 76 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 140 140 UDP-GlcNAc; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01631}.
BINDING 154 154 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 169 169 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 227 227 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 333 333 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631, ECO:0000269|Ref.4}.
BINDING 351 351 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631, ECO:0000269|Ref.4}.
BINDING 366 366 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631, ECO:0000269|Ref.4}.
BINDING 377 377 UDP-GlcNAc. {ECO:0000255|HAMAP-
Rule:MF_01631, ECO:0000269|Ref.4}.
BINDING 380 380 Acetyl-CoA; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01631}.
BINDING 405 405 Acetyl-CoA. {ECO:0000255|HAMAP-
Rule:MF_01631}.
BINDING 423 423 Acetyl-CoA; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01631}.
BINDING 440 440 Acetyl-CoA. {ECO:0000255|HAMAP-
Rule:MF_01631}.
STRAND 6 12 {ECO:0000244|PDB:4FCE}.
HELIX 17 19 {ECO:0000244|PDB:4FCE}.
HELIX 25 27 {ECO:0000244|PDB:4FCE}.
STRAND 28 30 {ECO:0000244|PDB:4FCE}.
HELIX 35 46 {ECO:0000244|PDB:4FCE}.
STRAND 51 57 {ECO:0000244|PDB:4FCE}.
HELIX 59 65 {ECO:0000244|PDB:4FCE}.
STRAND 73 75 {ECO:0000244|PDB:4FCE}.
HELIX 82 89 {ECO:0000244|PDB:4FCE}.
HELIX 90 92 {ECO:0000244|PDB:4FCE}.
STRAND 97 103 {ECO:0000244|PDB:4FCE}.
HELIX 111 120 {ECO:0000244|PDB:4FCE}.
STRAND 125 132 {ECO:0000244|PDB:4FCE}.
STRAND 141 145 {ECO:0000244|PDB:4FCE}.
STRAND 148 153 {ECO:0000244|PDB:4FCE}.
HELIX 155 157 {ECO:0000244|PDB:4FCE}.
HELIX 162 164 {ECO:0000244|PDB:4FCE}.
STRAND 167 176 {ECO:0000244|PDB:4FCE}.
HELIX 177 185 {ECO:0000244|PDB:4FCE}.
HELIX 200 207 {ECO:0000244|PDB:4FCE}.
STRAND 212 215 {ECO:0000244|PDB:4FCE}.
HELIX 220 223 {ECO:0000244|PDB:4FCE}.
HELIX 229 250 {ECO:0000244|PDB:4FCE}.
STRAND 253 255 {ECO:0000244|PDB:4FCE}.
HELIX 257 259 {ECO:0000244|PDB:4FCE}.
STRAND 260 268 {ECO:0000244|PDB:4FCE}.
STRAND 278 286 {ECO:0000244|PDB:4FCE}.
STRAND 297 300 {ECO:0000244|PDB:4FCE}.
STRAND 314 317 {ECO:0000244|PDB:4FCE}.
STRAND 328 332 {ECO:0000244|PDB:4FCE}.
STRAND 343 355 {ECO:0000244|PDB:4FCE}.
STRAND 360 372 {ECO:0000244|PDB:4FCE}.
STRAND 383 385 {ECO:0000244|PDB:4FCE}.
STRAND 395 397 {ECO:0000244|PDB:4FCE}.
STRAND 408 415 {ECO:0000244|PDB:4FCE}.
SEQUENCE 456 AA; 48840 MW; 30C8729567281E6A CRC64;
MSNSSMSVVI LAAGKGTRMY SDLPKVLHPL AGKPMVQHVI DAAMKLGAQH VHLVYGHGGE
LLKKTLADPS LNWVLQAEQL GTGHAMQQAA PHFADDEDIL MLYGDVPLIS VDTLQRLLAA
KPEGGIGLLT VKLDNPSGYG RIVRENGDVV GIVEHKDASD AQREINEINT GILVANGRDL
KRWLSLLDNN NAQGEFYITD IIALAHADGK KIATVHPTRL SEVEGVNNRL QLSALERVFQ
TEQAEKLLLA GVMLLDPSRF DLRGELTHGR DITIDTNVII EGHVILGDRV RIGTGCVLKN
CVIGDDSEIS PYTVLEDARL DANCTVGPFA RLRPGAELAE GAHVGNFVEI KKARLGKGSK
AGHLSYLGDA EIGAGVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVANGAT
IGAGTTVTRD VAENELVISR VKQVHIQGWK RPVKKK


Related products :

Catalog number Product name Quantity
E1540h Mouse ELISA Kit FOR Putative N-acetylglucosamine-6-phosphate deacetylase 96T
G5411 Putative N-acetylglucosamine-6-phosphate deacetylase (AMDHD2), Rat, ELISA Kit 96T
CSB-EL001660RA Rat Putative N-acetylglucosamine-6-phosphate deacetylase(AMDHD2) ELISA kit 96T
GPT_MOUSE Mouse ELISA Kit FOR UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase 96T
NAGA_BOVIN Bovine ELISA Kit FOR Putative N-acetylglucosamine-6-phosphate deacetylase 96T
CSB-EL001660MO Mouse Putative N-acetylglucosamine-6-phosphate deacetylase(AMDHD2) ELISA kit 96T
CSB-EL001660BO Bovine Putative N-acetylglucosamine-6-phosphate deacetylase(AMDHD2) ELISA kit 96T
GNRH2 GNPTG Gene N-acetylglucosamine-1-phosphate transferase, gamma subunit
CSB-EL007121BO Bovine UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit 96T
CSB-EL001660RA Rat Putative N-acetylglucosamine-6-phosphate deacetylase(AMDHD2) ELISA kit SpeciesRat 96T
I0600 UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1), Mouse, ELISA Kit 96T
CSB-EL001660HU Human Putative N-acetylglucosamine-6-phosphate deacetylase(AMDHD2) ELISA kit 96T
I0599 UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1), Human, ELISA Kit 96T
I0598 UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1), Bovine, ELISA Kit 96T
CSB-EL007121HU Human UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit 96T
G5410 Putative N-acetylglucosamine-6-phosphate deacetylase (AMDHD2), Mouse, ELISA Kit 96T
CSB-EL007121MO Mouse UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit 96T
G5408 Putative N-acetylglucosamine-6-phosphate deacetylase (AMDHD2), Bovine, ELISA Kit 96T
G5409 Putative N-acetylglucosamine-6-phosphate deacetylase (AMDHD2), Human, ELISA Kit 96T
CSB-EL007121MO Mouse UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit SpeciesMouse 96T
GNRH1 GNPTAB Gene N-acetylglucosamine-1-phosphate transferase, alpha and beta subunits
CSB-EL007121HU Human UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit SpeciesHuman 96T
CSB-EL001660HU Human Putative N-acetylglucosamine-6-phosphate deacetylase(AMDHD2) ELISA kit SpeciesHuman 96T
CSB-EL007121BO Bovine UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase(DPAGT1) ELISA kit SpeciesBovine 96T
NAGA_RAT ELISA Kit FOR Putative N-acetylglucosamine-6-phosphate deacetylase; organism: Rat; gene name: Amdhd2 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