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

Diacylglycerol acyltransferase/mycolyltransferase Ag85A (DGAT) (EC 2.3.1.122) (EC 2.3.1.20) (Acyl-CoA:diacylglycerol acyltransferase) (Antigen 85 complex A) (85A) (Ag85A) (Fibronectin-binding protein A) (Fbps A)

 A85A_MYCTU              Reviewed;         338 AA.
P9WQP3; D6MJP3; F2GDG3; P0A4V2; P17944; P17996;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
05-DEC-2018, entry version 26.
RecName: Full=Diacylglycerol acyltransferase/mycolyltransferase Ag85A;
Short=DGAT;
EC=2.3.1.122;
EC=2.3.1.20;
AltName: Full=Acyl-CoA:diacylglycerol acyltransferase;
AltName: Full=Antigen 85 complex A;
Short=85A;
Short=Ag85A;
AltName: Full=Fibronectin-binding protein A;
Short=Fbps A;
Flags: Precursor;
Name=fbpA; Synonyms=mpt44; OrderedLocusNames=Rv3804c;
ORFNames=MTV026.09c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=2506131;
Borremans M., de Wit L., Volckaert G., Ooms J., de Bruyn J.,
Huygen K., van Vooren J.P., Stelandre M., Verhofstadt R., Content J.;
"Cloning, sequence determination, and expression of a 32-kilodalton-
protein gene of Mycobacterium tuberculosis.";
Infect. Immun. 57:3123-3130(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, AND
DISULFIDE BOND.
STRAIN=ATCC 35801 / TMC 107 / Erdman;
PubMed=8757831;
Harth G., Lee B.Y., Wang J., Clemens D.L., Horwitz M.A.;
"Novel insights into the genetics, biochemistry, and
immunocytochemistry of the 30-kilodalton major extracellular protein
of Mycobacterium tuberculosis.";
Infect. Immun. 64:3038-3047(1996).
[3]
ERRATUM.
Harth G., Lee B.Y., Wang J., Clemens D.L., Horwitz M.A.;
Infect. Immun. 65:852-852(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C01;
PubMed=20223296; DOI=10.1016/j.meegid.2010.03.003;
Chuang P.C., Chen Y.M., Chen H.Y., Jou R.;
"Single nucleotide polymorphisms in cell wall biosynthesis-associated
genes and phylogeny of Mycobacterium tuberculosis lineages.";
Infect. Genet. Evol. 10:459-466(2010).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[6]
FUNCTION IN THE FIBRONECTIN BINDING.
PubMed=3141278;
Abou-Zeid C., Ratliff T.L., Wiker H.G., Harboe M., Bennedsen J.,
Rook G.A.;
"Characterization of fibronectin-binding antigens released by
Mycobacterium tuberculosis and Mycobacterium bovis BCG.";
Infect. Immun. 56:3046-3051(1988).
[7]
PROTEIN SEQUENCE OF 44-53.
PubMed=2403534;
Wiker H.G., Sletten K., Nagai S., Harboe M.;
"Evidence for three separate genes encoding the proteins of the
mycobacterial antigen 85 complex.";
Infect. Immun. 58:272-274(1990).
[8]
FUNCTION AS A MYCOLYLTRANSFERASE, AND DISRUPTION PHENOTYPE.
PubMed=12010501; DOI=10.1046/j.1365-2958.2002.02953.x;
Puech V., Guilhot C., Perez E., Tropis M., Armitige L.Y., Gicquel B.,
Daffe M.;
"Evidence for a partial redundancy of the fibronectin-binding proteins
for the transfer of mycoloyl residues onto the cell wall
arabinogalactan termini of Mycobacterium tuberculosis.";
Mol. Microbiol. 44:1109-1122(2002).
[9]
FUNCTION AS A MYCOLYLTRANSFERASE, AND NOMENCLATURE.
PubMed=9162010; DOI=10.1126/science.276.5317.1420;
Belisle J.T., Vissa V.D., Sievert T., Takayama K., Brennan P.J.,
Besra G.S.;
"Role of the major antigen of Mycobacterium tuberculosis in cell wall
biogenesis.";
Science 276:1420-1422(1997).
[10]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[12]
FUNCTION AS A DIACYLGLYCEROL ACYLTRANSFERASE, CATALYTIC ACTIVITY,
MUTAGENESIS OF SER-169, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
LOCATION, AND SUBSTRATE SPECIFICITY.
PubMed=21819455; DOI=10.1111/j.1365-2958.2011.07792.x;
Elamin A.A., Stehr M., Spallek R., Rohde M., Singh M.;
"The Mycobacterium tuberculosis Ag85A is a novel diacylglycerol
acyltransferase involved in lipid body formation.";
Mol. Microbiol. 81:1577-1592(2011).
[13]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 43-338, DISULFIDE BOND, AND
SUBUNIT.
PubMed=15192106; DOI=10.1074/jbc.M400811200;
Ronning D.R., Vissa V., Besra G.S., Belisle J.T., Sacchettini J.C.;
"Mycobacterium tuberculosis antigen 85A and 85C structures confirm
binding orientation and conserved substrate specificity.";
J. Biol. Chem. 279:36771-36777(2004).
-!- FUNCTION: The antigen 85 proteins (FbpA, FbpB, FbpC) are
responsible for the high affinity of mycobacteria for fibronectin,
a large adhesive glycoprotein, which facilitates the attachment of
M.tuberculosis to murine alveolar macrophages (AMs). They also
help to maintain the integrity of the cell wall by catalyzing the
transfer of mycolic acids to cell wall arabinogalactan, and
through the synthesis of alpha,alpha-trehalose dimycolate (TDM,
cord factor). They catalyze the transfer of a mycoloyl residue
from one molecule of alpha,alpha-trehalose monomycolate (TMM) to
another TMM, leading to the formation of TDM. FbpA mediates
triacylglycerol (TAG) formation with long-chain acyl-CoA as the
acyl donor and 1,2-dipalmitoyl-sn-glycerol (1,2-dipalmitin) as the
acyl acceptor. It has a preference for C26:0-CoA over C18:1-CoA.
{ECO:0000269|PubMed:12010501, ECO:0000269|PubMed:21819455,
ECO:0000269|PubMed:3141278, ECO:0000269|PubMed:9162010}.
-!- CATALYTIC ACTIVITY:
Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-
glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815,
ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615;
EC=2.3.1.20; Evidence={ECO:0000269|PubMed:21819455};
-!- CATALYTIC ACTIVITY:
Reaction=2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-
trehalose 6,6'-bismycolate + alpha,alpha-trehalose;
Xref=Rhea:RHEA:23472, ChEBI:CHEBI:16551, ChEBI:CHEBI:18195,
ChEBI:CHEBI:18234; EC=2.3.1.122;
Evidence={ECO:0000269|PubMed:21819455};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=306 uM for C26:0-CoA (with 1,2-dipalmitin as the acyl
acceptor and at 37 degrees Celsius)
{ECO:0000269|PubMed:21819455};
KM=390 uM for palmitoleoyl-CoA (with 1,2-dipalmitin as the acyl
acceptor and at 37 degrees Celsius)
{ECO:0000269|PubMed:21819455};
KM=540 uM for C18:0-CoA (with 1,2-dipalmitin as the acyl
acceptor and at 37 degrees Celsius)
{ECO:0000269|PubMed:21819455};
Vmax=3166 nmol/min/mg enzyme (at 37 degrees Celsius)
{ECO:0000269|PubMed:21819455};
Note=Kcat is 55.54 (min-1).;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15192106,
ECO:0000269|PubMed:8757831}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall. Cytoplasm.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene produce normally
mycoloylated cell wall components. {ECO:0000269|PubMed:12010501}.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
-!- SIMILARITY: Belongs to the mycobacterial A85 antigen 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; M27016; AAA50288.1; -; Genomic_DNA.
EMBL; U47335; AAC44295.1; -; Genomic_DNA.
EMBL; GQ150314; ADD50052.1; -; Genomic_DNA.
EMBL; AL123456; CCP46633.1; -; Genomic_DNA.
PIR; H70887; H70887.
RefSeq; NP_218321.1; NC_000962.3.
RefSeq; WP_003900759.1; NZ_NVQJ01000022.1.
PDB; 1SFR; X-ray; 2.70 A; A/B/C=43-338.
PDBsum; 1SFR; -.
ProteinModelPortal; P9WQP3; -.
SMR; P9WQP3; -.
STRING; 83332.Rv3804c; -.
MoonProt; P9WQP3; -.
PaxDb; P9WQP3; -.
EnsemblBacteria; CCP46633; CCP46633; Rv3804c.
GeneID; 886132; -.
KEGG; mtu:Rv3804c; -.
TubercuList; Rv3804c; -.
eggNOG; COG0627; LUCA.
KO; K18851; -.
OMA; AWARNDP; -.
PhylomeDB; P9WQP3; -.
BioCyc; MetaCyc:G185E-8100-MONOMER; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IDA:MTBBASE.
GO; GO:0050348; F:trehalose O-mycolyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0035375; F:zymogen binding; IPI:CAFA.
GO; GO:0044119; P:growth of symbiont in host cell; IMP:MTBBASE.
GO; GO:0044121; P:growth of symbiont in host organelle; IMP:MTBBASE.
GO; GO:0071769; P:mycolate cell wall layer assembly; IBA:GO_Central.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000801; Esterase_put.
InterPro; IPR006311; TAT_signal.
Pfam; PF00756; Esterase; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Cell wall; Complete proteome;
Cytoplasm; Direct protein sequencing; Disulfide bond;
Reference proteome; Secreted; Signal; Transferase.
SIGNAL 1 43 Tat-type signal. {ECO:0000255}.
CHAIN 44 338 Diacylglycerol
acyltransferase/mycolyltransferase Ag85A.
/FTId=PRO_0000000214.
REGION 85 86 Substrate binding. {ECO:0000250}.
REGION 101 111 Fibronectin-binding.
REGION 275 278 Substrate binding. {ECO:0000250}.
REGION 305 307 Substrate binding. {ECO:0000250}.
ACT_SITE 169 169 Nucleophile. {ECO:0000305}.
ACT_SITE 273 273 {ECO:0000250}.
ACT_SITE 305 305 {ECO:0000250}.
BINDING 169 169 Substrate. {ECO:0000250}.
BINDING 197 197 Substrate. {ECO:0000250}.
BINDING 282 282 Substrate. {ECO:0000250}.
DISULFID 130 135 {ECO:0000269|PubMed:15192106,
ECO:0000269|PubMed:8757831}.
MUTAGEN 169 169 S->A: Abolishes diacylglycerol
acyltransferase activity.
{ECO:0000269|PubMed:21819455}.
STRAND 44 46 {ECO:0000244|PDB:1SFR}.
STRAND 52 58 {ECO:0000244|PDB:1SFR}.
TURN 59 62 {ECO:0000244|PDB:1SFR}.
STRAND 63 70 {ECO:0000244|PDB:1SFR}.
STRAND 78 82 {ECO:0000244|PDB:1SFR}.
STRAND 89 91 {ECO:0000244|PDB:1SFR}.
HELIX 93 97 {ECO:0000244|PDB:1SFR}.
HELIX 100 104 {ECO:0000244|PDB:1SFR}.
STRAND 110 114 {ECO:0000244|PDB:1SFR}.
STRAND 129 131 {ECO:0000244|PDB:1SFR}.
STRAND 134 136 {ECO:0000244|PDB:1SFR}.
HELIX 140 145 {ECO:0000244|PDB:1SFR}.
HELIX 147 156 {ECO:0000244|PDB:1SFR}.
STRAND 160 168 {ECO:0000244|PDB:1SFR}.
HELIX 170 181 {ECO:0000244|PDB:1SFR}.
TURN 183 185 {ECO:0000244|PDB:1SFR}.
STRAND 186 193 {ECO:0000244|PDB:1SFR}.
HELIX 203 213 {ECO:0000244|PDB:1SFR}.
HELIX 219 223 {ECO:0000244|PDB:1SFR}.
HELIX 230 233 {ECO:0000244|PDB:1SFR}.
TURN 236 239 {ECO:0000244|PDB:1SFR}.
HELIX 240 246 {ECO:0000244|PDB:1SFR}.
STRAND 249 253 {ECO:0000244|PDB:1SFR}.
HELIX 267 289 {ECO:0000244|PDB:1SFR}.
STRAND 294 298 {ECO:0000244|PDB:1SFR}.
HELIX 307 316 {ECO:0000244|PDB:1SFR}.
HELIX 318 325 {ECO:0000244|PDB:1SFR}.
SEQUENCE 338 AA; 35686 MW; 57B1CF95D07D52C0 CRC64;
MQLVDRVRGA VTGMSRRLVV GAVGAALVSG LVGAVGGTAT AGAFSRPGLP VEYLQVPSPS
MGRDIKVQFQ SGGANSPALY LLDGLRAQDD FSGWDINTPA FEWYDQSGLS VVMPVGGQSS
FYSDWYQPAC GKAGCQTYKW ETFLTSELPG WLQANRHVKP TGSAVVGLSM AASSALTLAI
YHPQQFVYAG AMSGLLDPSQ AMGPTLIGLA MGDAGGYKAS DMWGPKEDPA WQRNDPLLNV
GKLIANNTRV WVYCGNGKPS DLGGNNLPAK FLEGFVRTSN IKFQDAYNAG GGHNGVFDFP
DSGTHSWEYW GAQLNAMKPD LQRALGATPN TGPAPQGA


Related products :

Catalog number Product name Quantity
EIAAB25116 2-acylglycerol O-acyltransferase 3,Acyl-CoA monoacylglycerol acyltransferase 3,DC7,DGAT2L7,Diacylglycerol acyltransferase 2-like protein 7,Diacylglycerol O-acyltransferase candidate 7,hDC7,Homo sapien
EIAAB25111 2-acylglycerol O-acyltransferase 1,Acyl-CoA monoacylglycerol acyltransferase 1,DC2,DGAT2L1,Diacylglycerol acyltransferase 2-like protein 1,Diacylglycerol O-acyltransferase candidate 2,hDC2,Homo sapien
EIAAB25115 2-acylglycerol O-acyltransferase 2,Acyl-CoA monoacylglycerol acyltransferase 2,DC5,DGAT2L5,Diacylglycerol acyltransferase 2-like protein 5,Diacylglycerol O-acyltransferase candidate 5,hDC5,hMGAT2,Homo
EIAAB25112 2-acylglycerol O-acyltransferase 1,Acyl-CoA monoacylglycerol acyltransferase 1,Dgat2l1,Diacylglycerol acyltransferase 2-like protein 1,MGAT1,Mogat1,Monoacylglycerol O-acyltransferase 1,Mouse,Mus muscu
EIAAB25114 2-acylglycerol O-acyltransferase 2,Acyl-CoA monoacylglycerol acyltransferase 2,Dgat2l5,Diacylglycerol acyltransferase 2-like protein 5,Mgat1l,MGAT2,Mogat2,Monoacylglycerol O-acyltransferase 1-like,Mon
EIAAB11040 Dgat,Dgat1,Diacylglycerol O-acyltransferase 1,Diglyceride acyltransferase,Mouse,Mus musculus
EIAAB11043 Dgat,Dgat1,Diacylglycerol O-acyltransferase 1,Diglyceride acyltransferase,Rat,Rattus norvegicus
EIAAB11036 DC3,DGAT2L6,Diacylglycerol O-acyltransferase 2-like protein 6,Diacylglycerol O-acyltransferase candidate 3,hDC3,Homo sapiens,Human
EIAAB11041 ACAT-related gene product 1,AGRP1,DGAT,DGAT1,Diacylglycerol O-acyltransferase 1,Diglyceride acyltransferase,Homo sapiens,Human
26-460 Dietary fat absorption from the small intestine is facilitated by acyl-CoA monoacylglycerol transferase (MOGAT) and acyl-CoA diacylglycerol acyltransferase (DGAT) activities. MOGAT catalyzes the joini 0.05 mg
15-288-22813 Antigen 85-A - 85A; Antigen 85 complex A; Ag85A; Mycolyl transferase 85A; EC 2.3.1.-; Fibronectin-binding protein A Polyclonal 0.05 mg
15-288-22813 Antigen 85-A - 85A; Antigen 85 complex A; Ag85A; Mycolyl transferase 85A; EC 2.3.1.-; Fibronectin-binding protein A Polyclonal 0.1 mg
AS12 1874 rabbit polyclonal DGAT2A | Acyl-CoA: Diacylglycerol acyltransferase 100
EIAAB11045 Bos taurus,Bovine,DGAT2,Diacylglycerol O-acyltransferase 2,Diglyceride acyltransferase 2
EIAAB11042 Bos taurus,Bovine,DGAT1,Diacylglycerol O-acyltransferase 1,Diglyceride acyltransferase
EIAAB11044 Dgat2,Diacylglycerol O-acyltransferase 2,Diglyceride acyltransferase 2,Rat,Rattus norvegicus
EIAAB11047 Dgat2,Diacylglycerol O-acyltransferase 2,Diglyceride acyltransferase 2,Mouse,Mus musculus
EIAAB11046 DGAT2,Diacylglycerol O-acyltransferase 2,Diglyceride acyltransferase 2,HMFN1045,Homo sapiens,Human,UNQ738_PRO1433
CSB-EL006819HU Human Diacylglycerol O-acyltransferase 2-like protein 6(DGAT2L6) ELISA kit 96T
EIAAB11038 Dgat2l6,Diacylglycerol O-acyltransferase 2-like protein 6,Mouse,Mus musculus
CSB-EL006819BO Bovine Diacylglycerol O-acyltransferase 2-like protein 6(DGAT2L6) ELISA kit 96T
CSB-EL006819MO Mouse Diacylglycerol O-acyltransferase 2-like protein 6(DGAT2L6) ELISA kit 96T
EIAAB11037 Bos taurus,Bovine,DGAT2L6,Diacylglycerol O-acyltransferase 2-like protein 6
CSB-EL006819BO Bovine Diacylglycerol O-acyltransferase 2-like protein 6(DGAT2L6) ELISA kit SpeciesBovine 96T
CSB-EL006819HU Human Diacylglycerol O-acyltransferase 2-like protein 6(DGAT2L6) ELISA kit SpeciesHuman 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





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