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

Endonuclease V (EC 3.2.2.17) (DNA-(apurinic or apyrimidinic site) lyase) (AP lyase) (EC 4.2.99.18) (T4 pyrimidine dimer glycosylase) (T4-Pdg)

 END5_BPT4               Reviewed;         138 AA.
P04418; D9IEF4;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 114.
RecName: Full=Endonuclease V {ECO:0000303|PubMed:16916523};
EC=3.2.2.17 {ECO:0000269|PubMed:6254991, ECO:0000269|PubMed:8347626};
AltName: Full=DNA-(apurinic or apyrimidinic site) lyase;
Short=AP lyase;
EC=4.2.99.18 {ECO:0000269|PubMed:6254991, ECO:0000269|PubMed:8347626};
AltName: Full=T4 pyrimidine dimer glycosylase {ECO:0000303|PubMed:16916523};
Short=T4-Pdg {ECO:0000303|PubMed:16916523};
Enterobacteria phage T4 (Bacteriophage T4).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
Tevenvirinae; T4virus.
NCBI_TaxID=10665;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6095188; DOI=10.1093/nar/12.21.8085;
Valerie K., Henderson E.E., Deriel J.K.;
"Identification, physical map location and sequence of the denV gene
from bacteriophage T4.";
Nucleic Acids Res. 12:8085-8096(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3024113; DOI=10.1093/nar/14.21.8637;
Valerie K., Stevens J., Lynch M., Henderson E.E., de Riel J.K.;
"Nucleotide sequence and analysis of the 58.3 to 65.5-kb early region
of bacteriophage T4.";
Nucleic Acids Res. 14:8637-8654(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6092716;
Radany E.H., Naumovski L., Love J.D., Gutekunst K.A., Hall D.H.,
Friedberg E.C.;
"Physical mapping and complete nucleotide sequence of the denV gene of
bacteriophage T4.";
J. Virol. 52:846-856(1984).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12626685; DOI=10.1128/MMBR.67.1.86-156.2003;
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
"Bacteriophage T4 genome.";
Microbiol. Mol. Biol. Rev. 67:86-156(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21029436; DOI=10.1186/1743-422X-7-292;
Petrov V.M., Ratnayaka S., Nolan J.M., Miller E.S., Karam J.D.;
"Genomes of the T4-related bacteriophages as windows on microbial
genome evolution.";
Virol. J. 7:292-292(2010).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=147 {ECO:0000312|EMBL:AHY83780.1},
GT7 {ECO:0000312|EMBL:AHY83971.1}, and
Wild {ECO:0000312|EMBL:AHY83587.1};
PubMed=26081634; DOI=10.1128/mBio.00648-15;
Bryson A.L., Hwang Y., Sherrill-Mix S., Wu G.D., Lewis J.D., Black L.,
Clark T.A., Bushman F.D.;
"Covalent Modification of Bacteriophage T4 DNA Inhibits CRISPR-Cas9.";
MBio 6:E00648-E00648(2015).
[7]
MUTAGENESIS OF GLU-11; HIS-16; TYR-21; ARG-22; GLU-23; ARG-26; ARG-40;
ARG-42; ARG-68; LYS-86; ASP-87; ARG-117; ASP-119; GLU-120; LYS-121;
ARG-125; TYR-129; TYR-132 AND LYS-134.
PubMed=1409651; DOI=10.1073/pnas.89.20.9420;
Doi T., Recktenwald A., Karaki Y., Kikuchi M., Morikawa K.,
Ikehara M., Inaoka T., Hori N., Ohtsuka E.;
"Role of the basic amino acid cluster and Glu-23 in pyrimidine dimer
glycosylase activity of T4 endonuclease V.";
Proc. Natl. Acad. Sci. U.S.A. 89:9420-9424(1992).
[8]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=8347626; DOI=10.1021/bi00083a032;
Dodson M.L., Schrock R.D. III, Lloyd R.S.;
"Evidence for an imino intermediate in the T4 endonuclease V
reaction.";
Biochemistry 32:8284-8290(1993).
[9]
MUTAGENESIS OF HIS-16.
PubMed=14610082; DOI=10.1074/jbc.M304714200;
Meador M.G., Rajagopalan L., Lloyd R.S., Dodson M.L.;
"Role of His-16 in turnover of T4 pyrimidine dimer glycosylase.";
J. Biol. Chem. 279:3348-3353(2004).
[10]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=6254991;
Gordon L.K., Haseltine W.A.;
"Comparison of the cleavage of pyrimidine dimers by the bacteriophage
T4 and Micrococcus luteus UV-specific endonucleases.";
J. Biol. Chem. 255:12047-12050(1980).
[11]
MUTAGENESIS OF GLU-23.
PubMed=1357629; DOI=10.1093/nar/20.18.4761;
Hori N., Doi T., Karaki Y., Kikuchi M., Ikehara M., Ohtsuka E.;
"Participation of glutamic acid 23 of T4 endonuclease V in the beta-
elimination reaction of an abasic site in a synthetic duplex DNA.";
Nucleic Acids Res. 20:4761-4764(1992).
[12]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed=1575827; DOI=10.1126/science.1575827;
Morikawa K., Matsumoto O., Tsujimoto M., Katayanagi K., Ariyoshi M.,
Doi T., Ikehara M., Inaoka T., Ohtsuka E.;
"X-ray structure of T4 endonuclease V: an excision repair enzyme
specific for a pyrimidine dimer.";
Science 256:523-526(1992).
[13] {ECO:0000244|PDB:1VAS}
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 2-138 IN COMPLEX WITH DNA,
AND ACTIVE SITE.
PubMed=8521494; DOI=10.1016/0092-8674(95)90190-6;
Vassylyev D.G., Kashiwagi T., Mikami Y., Ariyoshi M., Iwai S.,
Ohtsuka E., Morikawa K.;
"Atomic model of a pyrimidine dimer excision repair enzyme complexed
with a DNA substrate: structural basis for damaged DNA recognition.";
Cell 83:773-782(1995).
[14] {ECO:0000244|PDB:1ENI, ECO:0000244|PDB:1ENJ, ECO:0000244|PDB:1ENK, ECO:0000244|PDB:2END}
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
PubMed=7783199; DOI=10.1006/jmbi.1995.0302;
Morikawa K., Ariyoshi M., Vassylyev D.G., Matsumoto O., Katayanagi K.,
Ohtsuka E.;
"Crystal structure of a pyrimidine dimer-specific excision repair
enzyme from bacteriophage T4: refinement at 1.45 A and X-ray analysis
of the three active site mutants.";
J. Mol. Biol. 249:360-375(1995).
[15] {ECO:0000244|PDB:2FCC}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-138 IN COMPLEX WITH ABASIC
SITE-CONTAINING DNA, AND FUNCTION.
PubMed=16916523; DOI=10.1016/j.jmb.2006.06.059;
Golan G., Zharkov D.O., Grollman A.P., Dodson M.L., McCullough A.K.,
Lloyd R.S., Shoham G.;
"Structure of T4 pyrimidine dimer glycosylase in a reduced imine
covalent complex with abasic site-containing DNA.";
J. Mol. Biol. 362:241-258(2006).
-!- FUNCTION: Participates in the repair of UV-damaged DNA by excising
pyrimidine dimers that are the major UV-lesions (PubMed:6254991).
DNA glycosylase activity hydrolyzes the glycosylic bond of the 5'
pyrimidine of the dimer (PubMed:6254991). This leaves
apurinic/apyrimidic (AP) sites in the DNA. These AP sites are
removed by the AP lyase activity which cleaves the intrapyrimidine
phosphodiester bond (PubMed:6254991). Catalysis proceeds via a
protonated imine covalent intermediate between the alpha-amino
group of the N-terminal threonine residue and the C1' of the
deoxyribose sugar of the 5' pyrimidine at the dimer site
(PubMed:8347626) (PubMed:16916523). {ECO:0000269|PubMed:16916523,
ECO:0000269|PubMed:6254991, ECO:0000269|PubMed:8347626}.
-!- CATALYTIC ACTIVITY: Cleaves the N-glycosidic bond between the 5'-
pyrimidine residue in cyclobutadipyrimidine (in DNA) and the
corresponding deoxy-D-ribose residue. {ECO:0000269|PubMed:6254991,
ECO:0000269|PubMed:8347626}.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate. {ECO:0000269|PubMed:6254991,
ECO:0000269|PubMed:8347626}.
-!- SUBUNIT: Monomer.
-!- MISCELLANEOUS: Phage T4 deficient in the enzymes are extremely
sensitive to UV.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X04567; CAA28215.1; -; Genomic_DNA.
EMBL; AF158101; AAD42563.1; -; Genomic_DNA.
EMBL; HM137666; ADJ39840.1; -; Genomic_DNA.
EMBL; KJ477684; AHY83587.1; -; Genomic_DNA.
EMBL; KJ477685; AHY83780.1; -; Genomic_DNA.
EMBL; KJ477686; AHY83971.1; -; Genomic_DNA.
PIR; A93540; NEBPT4.
RefSeq; NP_049733.1; NC_000866.4.
PDB; 1ENI; X-ray; 2.20 A; A=1-138.
PDB; 1ENJ; X-ray; 1.80 A; A=1-138.
PDB; 1ENK; X-ray; 2.00 A; A=1-138.
PDB; 1VAS; X-ray; 2.75 A; A=2-138.
PDB; 2END; X-ray; 1.45 A; A=1-138.
PDB; 2FCC; X-ray; 2.30 A; A/B=2-138.
PDBsum; 1ENI; -.
PDBsum; 1ENJ; -.
PDBsum; 1ENK; -.
PDBsum; 1VAS; -.
PDBsum; 2END; -.
PDBsum; 2FCC; -.
ProteinModelPortal; P04418; -.
SMR; P04418; -.
GeneID; 1258606; -.
KEGG; vg:1258606; -.
KO; K21522; -.
OrthoDB; VOG09000111; -.
BRENDA; 3.1.25.1; 732.
EvolutionaryTrace; P04418; -.
Proteomes; UP000001092; Genome.
Proteomes; UP000009087; Genome.
Proteomes; UP000185269; Genome.
Proteomes; UP000185270; Genome.
Proteomes; UP000185271; Genome.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0140080; F:class III/IV DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
GO; GO:0033959; F:deoxyribodipyrimidine endonucleosidase activity; IEA:UniProtKB-EC.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0000704; F:pyrimidine dimer DNA N-glycosylase activity; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
Gene3D; 1.10.440.10; -; 1.
InterPro; IPR004260; Pyr-dimer_DNA_glycosylase.
InterPro; IPR021143; Pyr-dimer_DNAGlyclase_EndonucV.
InterPro; IPR024796; T4_endonuc_V.
Pfam; PF03013; Pyr_excise; 1.
PIRSF; PIRSF001000; PDG_ENDV; 1.
ProDom; PD021350; Pyr-dimer_DNA_glycosylase; 1.
SUPFAM; SSF47077; SSF47077; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA damage; DNA repair; Endonuclease;
Glycosidase; Hydrolase; Lyase; Multifunctional enzyme; Nuclease;
Reference proteome.
CHAIN 1 138 Endonuclease V.
/FTId=PRO_0000164934.
ACT_SITE 2 2 Nucleophile; via amide nitrogen.
{ECO:0000244|PDB:1VAS,
ECO:0000269|PubMed:8347626}.
ACT_SITE 23 23 Proton acceptor. {ECO:0000244|PDB:1VAS,
ECO:0000269|PubMed:8347626}.
SITE 3 3 Substrate binding.
{ECO:0000269|PubMed:1409651,
ECO:0000269|PubMed:7783199}.
SITE 22 22 Substrate binding.
{ECO:0000269|PubMed:1409651}.
SITE 26 26 Transition state stabilizer.
{ECO:0000244|PDB:1VAS}.
SITE 117 117 Substrate binding.
{ECO:0000269|PubMed:1409651}.
SITE 121 121 Substrate binding.
{ECO:0000269|PubMed:1409651}.
MUTAGEN 3 3 R->K: Complete loss of DNA glycosylase
activity. {ECO:0000305|PubMed:1409651}.
MUTAGEN 11 11 E->Q: 24% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 16 16 H->A: 30% decrease in enzymatic activity.
{ECO:0000269|PubMed:14610082}.
MUTAGEN 16 16 H->C: 40% decrease in enzymatic activity.
{ECO:0000269|PubMed:14610082}.
MUTAGEN 16 16 H->D: 60% decrease in enzymatic activity.
{ECO:0000269|PubMed:14610082}.
MUTAGEN 16 16 H->E: 50% decrease in enzymatic activity.
{ECO:0000269|PubMed:14610082}.
MUTAGEN 16 16 H->K: 75% decrease in enzymatic activity.
{ECO:0000269|PubMed:14610082}.
MUTAGEN 16 16 H->Q: 60% decrease in enzymatic activity.
{ECO:0000269|PubMed:1409651}.
MUTAGEN 16 16 H->S: 70% decrease in enzymatic activity.
{ECO:0000269|PubMed:14610082}.
MUTAGEN 21 21 Y->F: No effect on DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 22 22 R->Q: Almost complete loss of DNA
glycosylase activity.
{ECO:0000269|PubMed:1409651}.
MUTAGEN 23 23 E->D: Complete loss of DNA glycosylase
activity. No effect on AP lyase activity.
{ECO:0000269|PubMed:1357629,
ECO:0000269|PubMed:1409651}.
MUTAGEN 23 23 E->Q: Complete loss of DNA glycosylase
activity. Complete loss of AP lyase
activity. {ECO:0000269|PubMed:1357629,
ECO:0000269|PubMed:1409651}.
MUTAGEN 26 26 R->Q: Almost complete loss of DNA
glycosylase activity.
{ECO:0000269|PubMed:1409651}.
MUTAGEN 32 32 R->Q: 10% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 40 40 R->Q: 20% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 42 42 R->Q: 25% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 68 68 R->Q: 35% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 86 86 K->Q: No effect on DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 87 87 D->E: No effect on DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 87 87 D->N: 20% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 117 117 R->Q: 60% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 119 119 D->N: 5% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 120 120 E->Q: 10% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 121 121 K->Q: 90% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 125 125 R->Q: 10% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 129 129 Y->F: 65% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 132 132 Y->W: 10% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
MUTAGEN 134 134 K->Q: 20% decrease in DNA glycosylase
activity. {ECO:0000269|PubMed:1409651}.
HELIX 9 11 {ECO:0000244|PDB:2END}.
HELIX 14 23 {ECO:0000244|PDB:2END}.
HELIX 26 36 {ECO:0000244|PDB:2END}.
HELIX 41 43 {ECO:0000244|PDB:2END}.
TURN 54 57 {ECO:0000244|PDB:2END}.
HELIX 58 60 {ECO:0000244|PDB:2END}.
HELIX 64 80 {ECO:0000244|PDB:2END}.
HELIX 98 100 {ECO:0000244|PDB:2END}.
HELIX 108 124 {ECO:0000244|PDB:2END}.
HELIX 126 128 {ECO:0000244|PDB:2END}.
STRAND 131 133 {ECO:0000244|PDB:1ENJ}.
SEQUENCE 138 AA; 16079 MW; 90B889C8E6686697 CRC64;
MTRINLTLVS ELADQHLMAE YRELPRVFGA VRKHVANGKR VRDFKISPTF ILGAGHVTFF
YDKLEFLRKR QIELIAECLK RGFNIKDTTV QDISDIPQEF RGDYIPHEAS IAISQARLDE
KIAQRPTWYK YYGKAIYA


Related products :

Catalog number Product name Quantity
EIAAB26878 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Gm1212,Mouse,Mus musculus,NEH2,Nei homolog 2,Neil2,Nei-like protein 2
EIAAB26879 DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,Homo sapiens,Human,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26876 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,Mouse,Mus musculus,NEH1,Nei homolog 1,Nei1,Neil1,Nei-like protein 1
EIAAB26880 Bos taurus,Bovine,DNA glycosylase_AP lyase Neil2,DNA-(apurinic or apyrimidinic site) lyase Neil2,Endonuclease 8-like 2,Endonuclease VIII-like 2,NEH2,Nei homolog 2,NEIL2,Nei-like protein 2
EIAAB26877 DNA glycosylase_AP lyase Neil1,DNA-(apurinic or apyrimidinic site) lyase Neil1,Endonuclease 8-like 1,Endonuclease VIII-like 1,FPG1,Homo sapiens,Human,NEH1,Nei homolog 1,NEIL1,Nei-like protein 1
18-003-43959 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
18-003-43958 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN Polyclonal 0.1 mg Protein A
18-003-43422 DNA-(apurinic or apyrimidinic site) lyase - EC 4.2.99.18; AP endonuclease 1; APEX nuclease; APEN; Protein REF-1 Polyclonal 0.1 mg Protein A
EH2009 DNA-(apurinic or apyrimidinic site) lyase Elisa Kit 96T
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase 500ug
E14887d Mouse ELISA Kit FOR DNA-(apurinic or apyrimidinic site) lyase 2 96T
CSB-EL001900RA Rat DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
AE56100RA Rat DNA- (apurinic or apyrimidinic site) lyase (APEX1) ELISA Kit 48T
abx109730 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody 100 μg
CSB-EL001901HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001900HU Human DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001900MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
CSB-EL001901BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EL001900BO Bovine DNA-(apurinic or apyrimidinic site) lyase (APEX1) ELISA kit 96T
abx108186 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (HRP) 100 μg
CSB-EL001901MO Mouse DNA-(apurinic or apyrimidinic site) lyase (APEX2) ELISA kit 96T
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase Source: E.coli 200ug
CSB-EP001900HU Recombinant human DNA-(apurinic or apyrimidinic site) lyase Source: E.coli 1mg
abx106767 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (FITC) 100 μg
abx105348 Polyclonal Rabbit DNA-(apurinic or apyrimidinic site) lyase Antibody (Biotin) 100 μg


 

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