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

Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5'-phosphate synthase)

 PDXH_ECOLI              Reviewed;         218 AA.
P0AFI7; P28225;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-APR-2018, entry version 111.
RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase;
EC=1.4.3.5 {ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:7860596, ECO:0000269|PubMed:9693059};
AltName: Full=PNP/PMP oxidase;
Short=PNPOx;
AltName: Full=Pyridoxal 5'-phosphate synthase;
Name=pdxH; OrderedLocusNames=b1638, JW1630;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1356963; DOI=10.1128/jb.174.19.6033-6045.1992;
Lam H.-M., Winkler M.E.;
"Characterization of the complex pdxH-tyrS operon of Escherichia coli
K-12 and pleiotropic phenotypes caused by pdxH insertion mutations.";
J. Bacteriol. 174:6033-6045(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
STRAIN=K12;
PubMed=7860596; DOI=10.1128/jb.177.4.883-891.1995;
Zhao G., Winkler M.E.;
"Kinetic limitation and cellular amount of pyridoxine (pyridoxamine)
5'-phosphate oxidase of Escherichia coli K-12.";
J. Bacteriol. 177:883-891(1995).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
AND SUBUNIT.
PubMed=9693059; DOI=10.1006/prep.1998.0904;
di Salvo M., Yang E., Zhao G., Winkler M.E., Schirch V.;
"Expression, purification, and characterization of recombinant
Escherichia coli pyridoxine 5'-phosphate oxidase.";
Protein Expr. Purif. 13:349-356(1998).
[7]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-218 IN COMPLEX WITH FMN,
COFACTOR, AND SUBUNIT.
PubMed=10903950; DOI=10.1016/S0969-2126(00)00162-3;
Safo M.K., Mathews I., Musayev F.N., di Salvo M.L., Thiel D.J.,
Abraham D.J., Schirch V.;
"X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase
complexed with FMN at 1.8-A resolution.";
Structure 8:751-762(2000).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL
5'-PHOSPHATE AND FMN, COFACTOR, AND SUBUNIT.
PubMed=11453690; DOI=10.1006/jmbi.2001.4734;
Safo M.K., Musayev F.N., di Salvo M.L., Schirch V.;
"X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase
complexed with pyridoxal 5'-phosphate at 2.0 A resolution.";
J. Mol. Biol. 310:817-826(2001).
[9]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
5'-PHOSPHATE AND FMN, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-14; TYR-17; ASP-49;
ARG-197 AND HIS-199, AND COFACTOR.
PubMed=11786019; DOI=10.1006/jmbi.2001.5254;
di Salvo M.L., Ko T.-P., Musayev F.N., Raboni S., Schirch V.,
Safo M.K.;
"Active site structure and stereospecificity of Escherichia coli
pyridoxine-5'-phosphate oxidase.";
J. Mol. Biol. 315:385-397(2002).
[10]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
5'-PHOSPHATE AND FMN, COFACTOR, AND SUBUNIT.
PubMed=15858270; DOI=10.1107/S0907444905005512;
Safo M.K., Musayev F.N., Schirch V.;
"Structure of Escherichia coli pyridoxine 5'-phosphate oxidase in a
tetragonal crystal form: insights into the mechanistic pathway of the
enzyme.";
Acta Crystallogr. D 61:599-604(2005).
-!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-
phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal
5'-phosphate (PLP). {ECO:0000269|PubMed:11786019,
ECO:0000269|PubMed:7860596, ECO:0000269|PubMed:9693059}.
-!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) =
pyridoxal 5'-phosphate + NH(3) + H(2)O(2).
{ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:7860596,
ECO:0000269|PubMed:9693059}.
-!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-
phosphate + H(2)O(2). {ECO:0000269|PubMed:11786019,
ECO:0000269|PubMed:7860596, ECO:0000269|PubMed:9693059}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:10903950,
ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:11786019,
ECO:0000269|PubMed:15858270, ECO:0000269|PubMed:7860596,
ECO:0000269|PubMed:9693059};
Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:10903950,
ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:11786019,
ECO:0000269|PubMed:15858270, ECO:0000269|PubMed:7860596,
ECO:0000269|PubMed:9693059};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.3 uM for pyridoxamine 5'-phosphate
{ECO:0000269|PubMed:11786019};
KM=2 uM for pyridoxine 5'-phosphate (at pH 7.6 and 37 degrees
Celsius) {ECO:0000269|PubMed:7860596,
ECO:0000269|PubMed:9693059};
KM=105 uM for pyridoxamine 5'-phosphate (at pH 7.6 and 37
degrees Celsius) {ECO:0000269|PubMed:7860596};
Note=Kcat is 0.3 sec(-1) for oxidase activity with pyridoxine
5'-phosphate as substrate (at pH 7.6 and 37 degrees Celsius).
{ECO:0000269|PubMed:9693059};
-!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
-!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10903950,
ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:11786019,
ECO:0000269|PubMed:15858270, ECO:0000269|PubMed:7860596,
ECO:0000269|PubMed:9693059}.
-!- MISCELLANEOUS: Can bind a second molecule of pyridoxamine 5'-
phosphate at a non-catalytic site in a cleft at the protein
surface.
-!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M92351; AAA24709.1; -; Genomic_DNA.
EMBL; U00096; AAC74710.1; -; Genomic_DNA.
EMBL; AP009048; BAA15399.1; -; Genomic_DNA.
PIR; B43261; B43261.
RefSeq; NP_416155.1; NC_000913.3.
RefSeq; WP_001282319.1; NZ_LN832404.1.
PDB; 1DNL; X-ray; 1.80 A; A=20-218.
PDB; 1G76; X-ray; 2.20 A; A=1-218.
PDB; 1G77; X-ray; 2.10 A; A=1-218.
PDB; 1G78; X-ray; 2.20 A; A=1-218.
PDB; 1G79; X-ray; 2.00 A; A=1-218.
PDB; 1JNW; X-ray; 2.07 A; A=1-218.
PDB; 1WV4; X-ray; 2.60 A; A/B=1-218.
PDBsum; 1DNL; -.
PDBsum; 1G76; -.
PDBsum; 1G77; -.
PDBsum; 1G78; -.
PDBsum; 1G79; -.
PDBsum; 1JNW; -.
PDBsum; 1WV4; -.
ProteinModelPortal; P0AFI7; -.
SMR; P0AFI7; -.
BioGrid; 4263488; 16.
DIP; DIP-48024N; -.
IntAct; P0AFI7; 13.
STRING; 316385.ECDH10B_1772; -.
DrugBank; DB03345; Beta-Mercaptoethanol.
DrugBank; DB03247; Riboflavin Monophosphate.
EPD; P0AFI7; -.
PaxDb; P0AFI7; -.
PRIDE; P0AFI7; -.
EnsemblBacteria; AAC74710; AAC74710; b1638.
EnsemblBacteria; BAA15399; BAA15399; BAA15399.
GeneID; 946806; -.
KEGG; ecj:JW1630; -.
KEGG; eco:b1638; -.
PATRIC; fig|1411691.4.peg.622; -.
EchoBASE; EB1450; -.
EcoGene; EG11487; pdxH.
eggNOG; ENOG4108S7T; Bacteria.
eggNOG; COG0259; LUCA.
HOGENOM; HOG000242755; -.
InParanoid; P0AFI7; -.
KO; K00275; -.
OMA; PEPNAMV; -.
PhylomeDB; P0AFI7; -.
BioCyc; EcoCyc:PDXH-MONOMER; -.
BioCyc; MetaCyc:PDXH-MONOMER; -.
BRENDA; 1.4.3.5; 2026.
UniPathway; UPA01068; UER00304.
UniPathway; UPA01068; UER00305.
EvolutionaryTrace; P0AFI7; -.
PRO; PR:P0AFI7; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
GO; GO:0042301; F:phosphate ion binding; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IDA:EcoCyc.
GO; GO:1902444; F:riboflavin binding; IDA:CAFA.
GO; GO:0055114; P:oxidation-reduction process; IDA:EcoliWiki.
GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; EXP:EcoCyc.
GO; GO:0008615; P:pyridoxine biosynthetic process; IDA:EcoCyc.
Gene3D; 2.30.110.10; -; 1.
HAMAP; MF_01629; PdxH; 1.
InterPro; IPR000659; Pyridox_Oxase.
InterPro; IPR019740; Pyridox_Oxase_CS.
InterPro; IPR011576; Pyridox_Oxase_put.
InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
InterPro; IPR012349; Split_barrel_FMN-bd.
PANTHER; PTHR10851:SF0; PTHR10851:SF0; 1.
Pfam; PF10590; PNP_phzG_C; 1.
Pfam; PF01243; Putative_PNPOx; 1.
PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
TIGRFAMs; TIGR00558; pdxH; 1.
PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7860596}.
CHAIN 2 218 Pyridoxine/pyridoxamine 5'-phosphate
oxidase.
/FTId=PRO_0000167706.
NP_BIND 67 72 FMN. {ECO:0000269|PubMed:10903950,
ECO:0000269|PubMed:11453690,
ECO:0000269|PubMed:15858270}.
NP_BIND 82 83 FMN. {ECO:0000269|PubMed:10903950,
ECO:0000269|PubMed:11453690,
ECO:0000269|PubMed:15858270}.
NP_BIND 146 147 FMN. {ECO:0000269|PubMed:10903950,
ECO:0000269|PubMed:11453690,
ECO:0000269|PubMed:15858270}.
REGION 14 17 Substrate binding.
{ECO:0000269|PubMed:11786019}.
REGION 197 199 Substrate binding.
{ECO:0000269|PubMed:11786019}.
BINDING 72 72 Substrate. {ECO:0000269|PubMed:11453690}.
BINDING 88 88 FMN. {ECO:0000269|PubMed:10903950,
ECO:0000269|PubMed:11453690,
ECO:0000269|PubMed:15858270}.
BINDING 89 89 FMN. {ECO:0000269|PubMed:10903950,
ECO:0000269|PubMed:11453690,
ECO:0000269|PubMed:15858270}.
BINDING 111 111 FMN. {ECO:0000269|PubMed:11786019,
ECO:0000269|PubMed:15858270}.
BINDING 129 129 Substrate. {ECO:0000269|PubMed:11453690}.
BINDING 133 133 Substrate. {ECO:0000269|PubMed:11453690}.
BINDING 137 137 Substrate. {ECO:0000269|PubMed:11453690}.
BINDING 191 191 FMN. {ECO:0000269|PubMed:15858270}.
BINDING 201 201 FMN. {ECO:0000269|PubMed:11786019,
ECO:0000269|PubMed:15858270}.
MUTAGEN 14 14 R->E: Reduces affinity for substrate
about 7-fold, but has no effect on
catalytic activity.
{ECO:0000269|PubMed:11786019}.
MUTAGEN 14 14 R->M: Reduces affinity for substrate
about 9-fold, but has no effect on
catalytic activity.
{ECO:0000269|PubMed:11786019}.
MUTAGEN 17 17 Y->F: Reduces affinity for substrate 3-
fold, but has about 5-fold increase in
catalytic activity.
{ECO:0000269|PubMed:11786019}.
MUTAGEN 49 49 D->A: Reduces affinity for substrate 3-
fold and catalytic activity 2-fold.
{ECO:0000269|PubMed:11786019}.
MUTAGEN 197 197 R->E: Reduces affinity for substrate
8000-fold and catalytic activity 16-fold.
{ECO:0000269|PubMed:11786019}.
MUTAGEN 197 197 R->M: Reduces affinity for substrate 300-
fold and catalytic activity about 4-fold.
{ECO:0000269|PubMed:11786019}.
MUTAGEN 199 199 H->A: Reduces affinity for substrate 230-
fold, but has no effect on catalytic
activity. {ECO:0000269|PubMed:11786019}.
MUTAGEN 199 199 H->N: Reduces catalytic activity about 4-
fold, but has no effect on affinity for
substrate. {ECO:0000269|PubMed:11786019}.
HELIX 9 12 {ECO:0000244|PDB:1JNW}.
HELIX 24 26 {ECO:0000244|PDB:1DNL}.
HELIX 31 44 {ECO:0000244|PDB:1DNL}.
STRAND 52 58 {ECO:0000244|PDB:1DNL}.
STRAND 64 70 {ECO:0000244|PDB:1DNL}.
STRAND 73 75 {ECO:0000244|PDB:1DNL}.
STRAND 78 84 {ECO:0000244|PDB:1DNL}.
HELIX 88 95 {ECO:0000244|PDB:1DNL}.
STRAND 98 103 {ECO:0000244|PDB:1DNL}.
HELIX 106 108 {ECO:0000244|PDB:1DNL}.
STRAND 110 120 {ECO:0000244|PDB:1DNL}.
HELIX 123 130 {ECO:0000244|PDB:1DNL}.
HELIX 135 143 {ECO:0000244|PDB:1DNL}.
HELIX 154 166 {ECO:0000244|PDB:1DNL}.
STRAND 167 170 {ECO:0000244|PDB:1G79}.
STRAND 178 183 {ECO:0000244|PDB:1DNL}.
STRAND 186 192 {ECO:0000244|PDB:1DNL}.
HELIX 195 197 {ECO:0000244|PDB:1DNL}.
STRAND 200 206 {ECO:0000244|PDB:1DNL}.
STRAND 208 215 {ECO:0000244|PDB:1DNL}.
SEQUENCE 218 AA; 25545 MW; 8B47CEEEA6CEF5F9 CRC64;
MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP TAMVVATVDE
HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS LLFPWHTLER QVMVIGKAER
LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI SARGILESKF LELKQKFQQG EVPLPSFWGG
FRVSLEQIEF WQGGEHRLHD RFLYQRENDA WKIDRLAP


Related products :

Catalog number Product name Quantity
EIAAB31717 Homo sapiens,Human,PNPO,Pyridoxamine-phosphate oxidase,Pyridoxine-5'-phosphate oxidase
EIAAB31718 Bos taurus,Bovine,PNPO,Pyridoxamine-phosphate oxidase,Pyridoxine-5'-phosphate oxidase
EIAAB31719 Pnpo,Pyridoxamine-phosphate oxidase,Pyridoxine-5'-phosphate oxidase,Rat,Rattus norvegicus
EIAAB31720 Mouse,Mus musculus,Pnpo,Pyridoxamine-phosphate oxidase,Pyridoxine-5'-phosphate oxidase
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 1mg
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 5
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 20
REN-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 5
PNRC1 PNPO Gene pyridoxamine 5'-phosphate oxidase
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase PNPO 1mg
7-03395 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 20
7-03396 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 1mg
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase ENZYMES 5
ant-063 Mouse Anti Human Pyridoxamine 5'-Phosphate Oxidase 20
ant-063 Mouse Anti Human Pyridoxamine 5'-Phosphate Oxidase 5
ant-063 Mouse Anti Human Pyridoxamine 5'-Phosphate Oxidase 100
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase ENZYMES 20
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase ENZYMES 1mg
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase PNPO 20
OETENZ-030 Pyridoxamine 5'-Phosphate Oxidase Human Recombinant 5
7-03394 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase 5
201-20-4333 PNPO{pyridoxamine 5'-phosphate oxidase}rabbit.pAb 0.2ml
OETENZ-030 Pyridoxamine 5'-Phosphate Oxidase Human Recombinant 20
enz-030 Recombinant Human Pyridoxamine 5'-Phosphate Oxidase PNPO 5
RAN-063 Mouse Anti Human Pyridoxamine 5'-Phosphate Oxidase MONOCLONAL ANTIBODIES 5


 

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