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 B4GT1_BOVIN             Reviewed;         402 AA.
P08037; Q0VC05; Q8MIG0;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
05-JUL-2017, entry version 183.
RecName: Full=Beta-1,4-galactosyltransferase 1;
Short=Beta-1,4-GalTase 1;
Short=Beta4Gal-T1;
Short=b4Gal-T1;
EC=2.4.1.-;
AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1;
AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1;
Includes:
RecName: Full=Lactose synthase A protein;
EC=2.4.1.22;
Includes:
RecName: Full=N-acetyllactosamine synthase;
EC=2.4.1.90;
AltName: Full=Nal synthase;
Includes:
RecName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase;
EC=2.4.1.38;
Includes:
RecName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
EC=2.4.1.-;
Contains:
RecName: Full=Processed beta-1,4-galactosyltransferase 1;
Name=B4GALT1; Synonyms=GALT, GGTB2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2502398; DOI=10.1111/j.1432-1033.1989.tb14915.x;
D'Agostaro G., Bendiak B., Tropak M.;
"Cloning of cDNA encoding the membrane-bound form of bovine beta 1,4-
galactosyltransferase.";
Eur. J. Biochem. 183:211-217(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal skin;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-402.
PubMed=2419911; DOI=10.1073/pnas.83.6.1573;
Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R.,
Hollis G.F.;
"Bovine galactosyltransferase: identification of a clone by direct
immunological screening of a cDNA expression library.";
Proc. Natl. Acad. Sci. U.S.A. 83:1573-1577(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 74-402.
PubMed=3014508; DOI=10.1073/pnas.83.13.4720;
Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K.;
"Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-
4)galactosyltransferase.";
Proc. Natl. Acad. Sci. U.S.A. 83:4720-4724(1986).
[5]
SEQUENCE REVISION TO 164; 256 AND 265.
Qasba P.K., Narimatsu H., Masibay A.S.;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
PubMed=2503823; DOI=10.1073/pnas.86.15.5733;
Masibay A.S., Qasba P.K.;
"Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7
cells.";
Proc. Natl. Acad. Sci. U.S.A. 86:5733-5737(1989).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-165.
PubMed=2105947;
Russo R.N., Shaper N.L., Shaper J.H.;
"Bovine beta 1-->4-galactosyltransferase: two sets of mRNA transcripts
encode two forms of the protein with different amino-terminal domains.
In vitro translation experiments demonstrate that both the short and
the long forms of the enzyme are type II membrane-bound
glycoproteins.";
J. Biol. Chem. 265:3324-3331(1990).
[8]
PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-90.
PubMed=2117606;
Yadav S.P., Brew K.;
"Identification of a region of UDP-galactose:N-acetylglucosamine beta
4-galactosyltransferase involved in UDP-galactose binding by
differential labeling.";
J. Biol. Chem. 265:14163-14169(1990).
[9]
DISULFIDE BOND.
PubMed=1898734;
Yadav S.P., Brew K.;
"Structure and function in galactosyltransferase. Sequence locations
of alpha-lactalbumin binding site, thiol groups, and disulfide bond.";
J. Biol. Chem. 266:698-703(1991).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 115-402 IN COMPLEX WITH
SUBSTRATE, AND DISULFIDE BONDS.
PubMed=10393171; DOI=10.1093/emboj/18.13.3546;
Gastinel L.N., Cambillau C., Bourne Y.;
"Crystal structures of the bovine beta4galactosyltransferase catalytic
domain and its complex with uridine diphosphogalactose.";
EMBO J. 18:3546-3557(1999).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-402 IN COMPLEX WITH
SUBSTRATE AND MANGANESE IONS.
PubMed=11419947; DOI=10.1006/jmbi.2001.4757;
Ramakrishnan B., Qasba P.K.;
"Crystal structure of lactose synthase reveals a large conformational
change in its catalytic component, the beta1,4-galactosyltransferase-
I.";
J. Mol. Biol. 310:205-218(2001).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 117-402 IN COMPLEX WITH
SUBSTRATE AND MANGANESE IONS.
PubMed=12051854; DOI=10.1016/S0022-2836(02)00020-7;
Ramakrishnan B., Balaji P.V., Qasba P.K.;
"Crystal structure of beta1,4-galactosyltransferase complex with UDP-
Gal reveals an oligosaccharide acceptor binding site.";
J. Mol. Biol. 318:491-502(2002).
[13]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-402 OF MUTANT THR-342 IN
COMPLEX WITH SUBSTRATE AND MANGANESE IONS, AND MUTAGENESIS OF TRP-314.
PubMed=12927542; DOI=10.1016/S0022-2836(03)00790-3;
Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K.;
"The role of tryptophan 314 in the conformational changes of beta1,4-
galactosyltransferase-I.";
J. Mol. Biol. 331:1065-1076(2003).
-!- FUNCTION: The Golgi complex form catalyzes the production of
lactose in the lactating mammary gland and could also be
responsible for the synthesis of complex-type N-linked
oligosaccharides in many glycoproteins as well as the carbohydrate
moieties of glycolipids.
-!- FUNCTION: The cell surface form functions as a recognition
molecule during a variety of cell to cell and cell to matrix
interactions, as those occurring during development and egg
fertilization, by binding to specific oligosaccharide ligands on
opposing cells or in the extracellular matrix.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + D-glucose = UDP +
lactose.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-beta-D-
glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-
acetyl-beta-D-glucosaminylglycopeptide.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-D-glucosamine
= UDP + N-acetyllactosamine.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Homodimer; and heterodimer with alpha-lactalbumin to form
lactose synthase (PubMed:10393171, PubMed:11419947,
PubMed:12051854, PubMed:12927542). Interacts (via N-terminal
cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction
is direct (By similarity). {ECO:0000250|UniProtKB:P15535,
ECO:0000269|PubMed:10393171, ECO:0000269|PubMed:11419947,
ECO:0000269|PubMed:12051854, ECO:0000269|PubMed:12927542}.
-!- INTERACTION:
P29752:Lalba (xeno); NbExp=10; IntAct=EBI-1031436, EBI-1031454;
-!- SUBCELLULAR LOCATION: Isoform Long: Golgi apparatus, Golgi stack
membrane {ECO:0000250|UniProtKB:P15535}; Single-pass type II
membrane protein. Cell membrane; Single-pass type II membrane
protein. Cell surface. Cell projection, filopodium
{ECO:0000250|UniProtKB:P15535}. Note=Found in trans cisternae of
Golgi. B4GALT1 cell surface expression is regulated by UBE2Q1 (By
similarity). {ECO:0000250|UniProtKB:P15535}.
-!- SUBCELLULAR LOCATION: Isoform Short: Golgi apparatus, Golgi stack
membrane; Single-pass type II membrane protein. Note=Found in
trans cisternae of Golgi.
-!- SUBCELLULAR LOCATION: Processed beta-1,4-galactosyltransferase 1:
Secreted. Note=Soluble form found in body fluids.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Long; Synonyms=Cell surface;
IsoId=P08037-1; Sequence=Displayed;
Name=Short; Synonyms=Golgi complex;
IsoId=P08037-2; Sequence=VSP_018801;
-!- PTM: The soluble form derives from the membrane forms by
proteolytic processing.
-!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X14558; CAA32695.1; -; mRNA.
EMBL; BC120415; AAI20416.1; -; mRNA.
EMBL; M13214; AAA30534.1; -; mRNA.
EMBL; AF515786; AAM54035.2; -; mRNA.
EMBL; M25398; AAA30533.1; -; Genomic_DNA.
EMBL; J05217; AAA30559.1; -; mRNA.
PIR; I45897; I45897.
PIR; S05018; S05018.
RefSeq; NP_803478.1; NM_177512.2.
UniGene; Bt.5141; -.
PDB; 1FGX; X-ray; 2.40 A; A/B=115-402.
PDB; 1FR8; X-ray; 2.40 A; A/B=115-402.
PDB; 1NF5; X-ray; 2.00 A; B/D=130-402.
PDB; 1NHE; X-ray; 2.50 A; B/D=130-402.
PDB; 1NKH; X-ray; 2.00 A; B/D=130-402.
PDB; 1NMM; X-ray; 2.00 A; B/D=130-402.
PDB; 1NQI; X-ray; 2.00 A; B/D=130-402.
PDB; 1NWG; X-ray; 2.32 A; B/D=130-402.
PDB; 1O0R; X-ray; 2.30 A; A/B=130-402.
PDB; 1O23; X-ray; 2.32 A; B/D=130-402.
PDB; 1OQM; X-ray; 2.10 A; B/D=130-402.
PDB; 1PZT; X-ray; 1.92 A; A=130-402.
PDB; 1PZY; X-ray; 2.30 A; B/D=130-402.
PDB; 1TVY; X-ray; 2.30 A; A/B=130-402.
PDB; 1TW1; X-ray; 2.30 A; A/B=130-402.
PDB; 1TW5; X-ray; 2.30 A; A/B=130-402.
PDB; 1YRO; X-ray; 1.90 A; B/D=130-402.
PDB; 2FYC; X-ray; 2.00 A; B/D=130-402.
PDB; 2FYD; X-ray; 2.00 A; B/D=130-400.
PDB; 4KRV; X-ray; 2.40 A; A/B=130-402.
PDBsum; 1FGX; -.
PDBsum; 1FR8; -.
PDBsum; 1NF5; -.
PDBsum; 1NHE; -.
PDBsum; 1NKH; -.
PDBsum; 1NMM; -.
PDBsum; 1NQI; -.
PDBsum; 1NWG; -.
PDBsum; 1O0R; -.
PDBsum; 1O23; -.
PDBsum; 1OQM; -.
PDBsum; 1PZT; -.
PDBsum; 1PZY; -.
PDBsum; 1TVY; -.
PDBsum; 1TW1; -.
PDBsum; 1TW5; -.
PDBsum; 1YRO; -.
PDBsum; 2FYC; -.
PDBsum; 2FYD; -.
PDBsum; 4KRV; -.
ProteinModelPortal; P08037; -.
SMR; P08037; -.
IntAct; P08037; 1.
STRING; 9913.ENSBTAP00000020286; -.
BindingDB; P08037; -.
ChEMBL; CHEMBL3214; -.
CAZy; GT7; Glycosyltransferase Family 7.
MoonProt; P08037; -.
PaxDb; P08037; -.
PeptideAtlas; P08037; -.
PRIDE; P08037; -.
Ensembl; ENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249. [P08037-2]
GeneID; 281781; -.
KEGG; bta:281781; -.
CTD; 2683; -.
eggNOG; KOG3916; Eukaryota.
eggNOG; ENOG410ZYYA; LUCA.
GeneTree; ENSGT00760000119140; -.
HOGENOM; HOG000231027; -.
HOVERGEN; HBG058334; -.
InParanoid; P08037; -.
KO; K07966; -.
OMA; AHTRETM; -.
OrthoDB; EOG091G0P66; -.
TreeFam; TF312834; -.
BRENDA; 2.4.1.133; 908.
Reactome; R-BTA-1300644; Interaction With The Zona Pellucida.
Reactome; R-BTA-2022854; Keratan sulfate biosynthesis.
Reactome; R-BTA-5653890; Lactose synthesis.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-975577; N-Glycan antennae elongation.
SABIO-RK; P08037; -.
UniPathway; UPA00378; -.
EvolutionaryTrace; P08037; -.
Proteomes; UP000009136; Chromosome 8.
Bgee; ENSBTAG00000015249; -.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
GO; GO:0030057; C:desmosome; ISS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000138; C:Golgi trans cisterna; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0004461; F:lactose synthase activity; ISS:UniProtKB.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0035250; F:UDP-galactosyltransferase activity; ISS:UniProtKB.
GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
GO; GO:0045136; P:development of secondary sexual characteristics; IEA:Ensembl.
GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0006012; P:galactose metabolic process; IEA:Ensembl.
GO; GO:0005989; P:lactose biosynthetic process; IDA:CAFA.
GO; GO:0050900; P:leukocyte migration; IEA:Ensembl.
GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0009312; P:oligosaccharide biosynthetic process; ISS:UniProtKB.
GO; GO:0007341; P:penetration of zona pellucida; IEA:Ensembl.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IEA:Ensembl.
GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl.
GO; GO:0042125; P:protein galactosylation; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0006487; P:protein N-linked glycosylation; IDA:CAFA.
GO; GO:0060046; P:regulation of acrosome reaction; IEA:Ensembl.
GO; GO:0051270; P:regulation of cellular component movement; IEA:Ensembl.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR003859; Galactosyl_T.
InterPro; IPR027791; Galactosyl_T_C.
InterPro; IPR027995; Galactosyl_T_N.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR19300; PTHR19300; 1.
Pfam; PF02709; Glyco_transf_7C; 1.
Pfam; PF13733; Glyco_transf_7N; 1.
PRINTS; PR02050; B14GALTRFASE.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese;
Membrane; Metal-binding; Reference proteome; Secreted; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 402 Beta-1,4-galactosyltransferase 1.
/FTId=PRO_0000012276.
CHAIN ? 402 Processed beta-1,4-galactosyltransferase
1.
/FTId=PRO_0000296228.
TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.
TRANSMEM 25 44 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 45 402 Lumenal. {ECO:0000255}.
REGION 187 191 UDP-alpha-D-galactose binding.
REGION 226 228 UDP-alpha-D-galactose binding.
REGION 253 254 UDP-alpha-D-galactose binding.
REGION 316 319 N-acetyl-D-glucosamine binding.
REGION 347 349 UDP-alpha-D-galactose binding.
METAL 254 254 Manganese.
METAL 347 347 Manganese; via tele nitrogen.
BINDING 314 314 UDP-alpha-D-galactose.
BINDING 359 359 N-acetyl-D-glucosamine.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:2117606}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 134 176
DISULFID 247 266
VAR_SEQ 1 13 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_018801.
MUTAGEN 314 314 W->A: Reduces galactosyltransferase
activity, lactose synthase activity and
substrate binding by 99%.
{ECO:0000269|PubMed:12927542}.
CONFLICT 65 66 HG -> QA (in Ref. 7). {ECO:0000305}.
CONFLICT 158 158 V -> I (in Ref. 1; CAA32695).
{ECO:0000305}.
CONFLICT 187 187 P -> L (in Ref. 1; CAA32695).
{ECO:0000305}.
CONFLICT 205 206 IL -> MV (in Ref. 1; CAA32695).
{ECO:0000305}.
CONFLICT 282 282 F -> L (in Ref. 3; AAA30534).
{ECO:0000305}.
STRAND 149 151 {ECO:0000244|PDB:1TVY}.
HELIX 155 161 {ECO:0000244|PDB:1YRO}.
TURN 167 169 {ECO:0000244|PDB:1YRO}.
STRAND 174 177 {ECO:0000244|PDB:1YRO}.
STRAND 181 190 {ECO:0000244|PDB:1YRO}.
HELIX 192 208 {ECO:0000244|PDB:1YRO}.
STRAND 212 220 {ECO:0000244|PDB:1YRO}.
STRAND 222 224 {ECO:0000244|PDB:1YRO}.
HELIX 228 242 {ECO:0000244|PDB:1YRO}.
STRAND 247 251 {ECO:0000244|PDB:1YRO}.
STRAND 255 259 {ECO:0000244|PDB:1YRO}.
HELIX 278 280 {ECO:0000244|PDB:1YRO}.
STRAND 292 297 {ECO:0000244|PDB:1YRO}.
HELIX 298 303 {ECO:0000244|PDB:1YRO}.
STRAND 313 316 {ECO:0000244|PDB:1YRO}.
HELIX 317 327 {ECO:0000244|PDB:1YRO}.
TURN 337 340 {ECO:0000244|PDB:1YRO}.
STRAND 341 344 {ECO:0000244|PDB:1YRO}.
TURN 347 349 {ECO:0000244|PDB:1FR8}.
HELIX 351 353 {ECO:0000244|PDB:1NF5}.
HELIX 359 364 {ECO:0000244|PDB:1YRO}.
HELIX 366 369 {ECO:0000244|PDB:1YRO}.
TURN 370 372 {ECO:0000244|PDB:1YRO}.
HELIX 375 377 {ECO:0000244|PDB:1YRO}.
STRAND 381 387 {ECO:0000244|PDB:1YRO}.
STRAND 392 397 {ECO:0000244|PDB:1YRO}.
SEQUENCE 402 AA; 44843 MW; FABF94E74E0C6F81 CRC64;
MKFREPLLGG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLRRL PQLVGVHPPL
QGSSHGAAAI GQPSGELRLR GVAPPPPLQN SSKPRSRAPS NLDAYSHPGP GPGPGSNLTS
APVPSTTTRS LTACPEESPL LVGPMLIEFN IPVDLKLVEQ QNPKVKLGGR YTPMDCISPH
KVAIIIPFRN RQEHLKYWLY YLHPILQRQQ LDYGIYVINQ AGESMFNRAK LLNVGFKEAL
KDYDYNCFVF SDVDLIPMND HNTYRCFSQP RHISVAMDKF GFSLPYVQYF GGVSALSKQQ
FLSINGFPNN YWGWGGEDDD IYNRLAFRGM SVSRPNAVIG KCRMIRHSRD KKNEPNPQRF
DRIAHTKETM LSDGLNSLTY MVLEVQRYPL YTKITVDIGT PS


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