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

Photosystem II reaction center protein Z (PSII-Z)

 PSBZ_THEEB              Reviewed;          62 AA.
Q8DHJ2;
30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-FEB-2018, entry version 104.
RecName: Full=Photosystem II reaction center protein Z {ECO:0000255|HAMAP-Rule:MF_00644};
Short=PSII-Z {ECO:0000255|HAMAP-Rule:MF_00644};
Name=psbZ {ECO:0000255|HAMAP-Rule:MF_00644};
OrderedLocusNames=tsr1967;
Thermosynechococcus elongatus (strain BP-1).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Thermosynechococcus.
NCBI_TaxID=197221;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BP-1;
PubMed=12240834; DOI=10.1093/dnares/9.4.123;
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
DNA Res. 9:123-130(2002).
[2]
PROTEIN SEQUENCE OF 1-15, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y.,
Satoh K., Sugiura M.;
"Ycf12 is a core subunit in the photosystem II complex.";
Biochim. Biophys. Acta 1767:1269-1275(2007).
[3]
PROTEIN SEQUENCE OF 1-10, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR
LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=17967798; DOI=10.1093/pcp/pcm148;
Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M.;
"Absence of the PsbZ subunit prevents association of PsbK and Ycf12
with the PSII complex in the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
Plant Cell Physiol. 48:1758-1763(2007).
[4] {ECO:0000312|PDB:1S5L}
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=14764885; DOI=10.1126/science.1093087;
Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
"Architecture of the photosynthetic oxygen-evolving center.";
Science 303:1831-1838(2004).
[5]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=16355230; DOI=10.1038/nature04224;
Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
"Towards complete cofactor arrangement in the 3.0 A resolution
structure of photosystem II.";
Nature 438:1040-1044(2005).
[6]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, MASS
SPECTROMETRY, AND TOPOLOGY.
STRAIN=BP-1;
PubMed=19219048; DOI=10.1038/nsmb.1559;
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
"Cyanobacterial photosystem II at 2.9-A resolution and the role of
quinones, lipids, channels and chloride.";
Nat. Struct. Mol. Biol. 16:334-342(2009).
[7]
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND
MASS SPECTROMETRY.
STRAIN=BP-1;
PubMed=20558739; DOI=10.1074/jbc.M110.127589;
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
Zouni A.;
"Crystal structure of monomeric photosystem II from
Thermosynechococcus elongatus at 3.6 A resolution.";
J. Biol. Chem. 285:26255-26262(2010).
[8]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=21367867; DOI=10.1074/jbc.M110.215970;
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J.,
Kern J., Muh F., Dau H., Saenger W., Zouni A.;
"Structural basis of cyanobacterial photosystem II inhibition by the
herbicide terbutryn.";
J. Biol. Chem. 286:15964-15972(2011).
[9]
X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=22665786; DOI=10.1073/pnas.1204598109;
Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J.,
McQueen T.A., DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A.,
Schafer D.W., Seibert M.M., Sokaras D., Weng T.C., Zwart P.H.,
White W.E., Adams P.D., Bogan M.J., Boutet S., Williams G.J.,
Messinger J., Sauter N.K., Zouni A., Bergmann U., Yano J.,
Yachandra V.K.;
"Room temperature femtosecond X-ray diffraction of photosystem II
microcrystals.";
Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
[10]
X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=23413188; DOI=10.1126/science.1234273;
Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
Glockner C., Hellmich J., Laksmono H., Sierra R.G.,
Lassalle-Kaiser B., Koroidov S., Lampe A., Han G., Gul S., Difiore D.,
Milathianaki D., Fry A.R., Miahnahri A., Schafer D.W.,
Messerschmidt M., Seibert M.M., Koglin J.E., Sokaras D., Weng T.C.,
Sellberg J., Latimer M.J., Grosse-Kunstleve R.W., Zwart P.H.,
White W.E., Glatzel P., Adams P.D., Bogan M.J., Williams G.J.,
Boutet S., Messinger J., Zouni A., Sauter N.K., Yachandra V.K.,
Bergmann U., Yano J.;
"Simultaneous femtosecond X-ray spectroscopy and diffraction of
photosystem II at room temperature.";
Science 340:491-495(2013).
[11]
X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=25043005; DOI=10.1038/nature13453;
Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A.,
Rendek K.N., Hunter M.S., Shoeman R.L., White T.A., Wang D., James D.,
Yang J.H., Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A.,
Aquila A.L., Deponte D., Kirian R.A., Bari S., Bergkamp J.J.,
Beyerlein K.R., Bogan M.J., Caleman C., Chao T.C., Conrad C.E.,
Davis K.M., Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S.,
Laksmono H., Liang M., Lomb L., Marchesini S., Martin A.V.,
Messerschmidt M., Milathianaki D., Nass K., Ros A., Roy-Chowdhury S.,
Schmidt K., Seibert M., Steinbrener J., Stellato F., Yan L., Yoon C.,
Moore T.A., Moore A.L., Pushkar Y., Williams G.J., Boutet S.,
Doak R.B., Weierstall U., Frank M., Chapman H.N., Spence J.C.,
Fromme P.;
"Serial time-resolved crystallography of photosystem II using a
femtosecond X-ray laser.";
Nature 513:261-265(2014).
[12]
X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=25006873; DOI=10.1038/ncomms5371;
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S.,
Stan C.A., Gloeckner C., Lampe A., DiFiore D., Milathianaki D.,
Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D.,
Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M.,
Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A.,
Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.;
"Taking snapshots of photosynthetic water oxidation using femtosecond
X-ray diffraction and spectroscopy.";
Nat. Commun. 5:4371-4371(2014).
-!- FUNCTION: Controls the interaction of photosystem II (PSII) cores
with the light-harvesting antenna. May also aid in binding of
PsbK, Ycf12 and the oxygen-evolving complex to PSII, at least in
vitro. PSII is a light-driven water plastoquinone oxidoreductase,
using light energy to abstract electrons from H(2)O, generating a
proton gradient subsequently used for ATP formation.
{ECO:0000255|HAMAP-Rule:MF_00644, ECO:0000269|PubMed:17967798,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:25006873}.
-!- COFACTOR:
Note=PSII binds multiple chlorophylls, carotenoids and specific
lipids. {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
ECO:0000269|PubMed:25043005};
-!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of
membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI,
PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3
peripheral proteins PsbO, PsbU, PsbV and a large number of
cofactors. It forms dimeric complexes.
{ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
ECO:0000269|PubMed:25043005}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_00644, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
ECO:0000269|PubMed:17967798, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}; Multi-
pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00644,
ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
ECO:0000269|PubMed:25043005}. Note=Associated with the photosystem
II complex.
-!- MASS SPECTROMETRY: Mass=6798; Mass_error=5; Method=MALDI; Range=1-
62; Evidence={ECO:0000269|PubMed:19219048};
-!- MASS SPECTROMETRY: Mass=6793; Method=MALDI; Range=1-62;
Evidence={ECO:0000269|PubMed:20558739};
-!- DISRUPTION PHENOTYPE: Cells grow normally under all light regimes
tested; it is dispensable for photoautotrophic growth. The
deletion strain is more tolerant to photoinhibition, while
isolated PSII complex contains less PsbK and Ycf12 than wild-type
and also has reduced oxygen-evolving capacity.
{ECO:0000269|PubMed:17967798}.
-!- SIMILARITY: Belongs to the PsbZ family. {ECO:0000255|HAMAP-
Rule:MF_00644}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BA000039; BAC09519.1; -; Genomic_DNA.
RefSeq; NP_682757.1; NC_004113.1.
RefSeq; WP_011057802.1; NC_004113.1.
PDB; 1S5L; X-ray; 3.50 A; Z/z=1-62.
PDB; 2AXT; X-ray; 3.00 A; Z/z=1-62.
PDB; 3KZI; X-ray; 3.60 A; Z=1-62.
PDB; 4FBY; X-ray; 6.56 A; Z/l=1-62.
PDB; 4IXQ; X-ray; 5.70 A; Z/z=1-62.
PDB; 4IXR; X-ray; 5.90 A; Z/z=1-62.
PDB; 4PBU; X-ray; 5.00 A; Z/z=1-62.
PDB; 4PJ0; X-ray; 2.44 A; Z/z=1-62.
PDB; 4RVY; X-ray; 5.50 A; Z/z=1-62.
PDB; 4TNH; X-ray; 4.90 A; Z/z=1-62.
PDB; 4TNI; X-ray; 4.60 A; Z/z=1-62.
PDB; 4TNJ; X-ray; 4.50 A; Z/z=1-62.
PDB; 4TNK; X-ray; 5.20 A; Z/z=1-62.
PDB; 4V62; X-ray; 2.90 A; AZ/BZ=1-62.
PDB; 4V82; X-ray; 3.20 A; AZ/BZ=1-62.
PDB; 5E79; X-ray; 3.50 A; Z/z=1-62.
PDB; 5E7C; X-ray; 4.50 A; Z/z=1-62.
PDB; 5H2F; X-ray; 2.20 A; Z/z=1-62.
PDB; 5KAF; X-ray; 3.00 A; Z/z=1-62.
PDB; 5KAI; X-ray; 2.80 A; Z/z=1-62.
PDB; 5MX2; X-ray; 2.20 A; Z/z=1-62.
PDB; 5TIS; X-ray; 2.25 A; Z/z=1-62.
PDBsum; 1S5L; -.
PDBsum; 2AXT; -.
PDBsum; 3KZI; -.
PDBsum; 4FBY; -.
PDBsum; 4IXQ; -.
PDBsum; 4IXR; -.
PDBsum; 4PBU; -.
PDBsum; 4PJ0; -.
PDBsum; 4RVY; -.
PDBsum; 4TNH; -.
PDBsum; 4TNI; -.
PDBsum; 4TNJ; -.
PDBsum; 4TNK; -.
PDBsum; 4V62; -.
PDBsum; 4V82; -.
PDBsum; 5E79; -.
PDBsum; 5E7C; -.
PDBsum; 5H2F; -.
PDBsum; 5KAF; -.
PDBsum; 5KAI; -.
PDBsum; 5MX2; -.
PDBsum; 5TIS; -.
ProteinModelPortal; Q8DHJ2; -.
SMR; Q8DHJ2; -.
DIP; DIP-48504N; -.
IntAct; Q8DHJ2; 1.
STRING; 197221.tsr1967; -.
EnsemblBacteria; BAC09519; BAC09519; BAC09519.
GeneID; 1010256; -.
KEGG; tel:tsr1967; -.
PATRIC; fig|197221.4.peg.2057; -.
eggNOG; ENOG4105ZDH; Bacteria.
eggNOG; ENOG4112722; LUCA.
HOGENOM; HOG000264225; -.
KO; K02724; -.
OMA; QNWDQSK; -.
OrthoDB; POG091H14QX; -.
BioCyc; TELO197221:G1G3I-2000-MONOMER; -.
EvolutionaryTrace; Q8DHJ2; -.
Proteomes; UP000000440; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
Gene3D; 1.10.287.740; -; 1.
HAMAP; MF_00644; PSII_PsbZ; 1.
InterPro; IPR002644; PSII_PsbZ.
InterPro; IPR036512; PSII_PsbZ_sf.
PANTHER; PTHR34971; PTHR34971; 1.
Pfam; PF01737; Ycf9; 1.
ProDom; PD004770; PSII_PsbZ; 1.
SUPFAM; SSF161055; SSF161055; 1.
TIGRFAMs; TIGR03043; PS_II_psbZ; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Formylation; Membrane; Photosynthesis; Photosystem II;
Reaction center; Reference proteome; Thylakoid; Transmembrane;
Transmembrane helix.
CHAIN 1 62 Photosystem II reaction center protein Z.
/FTId=PRO_0000217733.
TOPO_DOM 1 10 Lumenal.
TRANSMEM 11 24 Helical. {ECO:0000255|HAMAP-
Rule:MF_00644,
ECO:0000269|PubMed:19219048}.
TOPO_DOM 25 38 Cytoplasmic.
{ECO:0000269|PubMed:19219048}.
TRANSMEM 39 53 Helical. {ECO:0000255|HAMAP-
Rule:MF_00644,
ECO:0000269|PubMed:19219048}.
TOPO_DOM 54 62 Lumenal. {ECO:0000269|PubMed:19219048}.
MOD_RES 1 1 N-formylmethionine.
{ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739}.
HELIX 2 27 {ECO:0000244|PDB:5H2F}.
STRAND 30 32 {ECO:0000244|PDB:4PJ0}.
HELIX 33 58 {ECO:0000244|PDB:5H2F}.
TURN 59 61 {ECO:0000244|PDB:5TIS}.
SEQUENCE 62 AA; 6764 MW; 313A629F73715DD8 CRC64;
MTILFQLALA ALVILSFVMV IGVPVAYASP QDWDRSKQLI FLGSGLWIAL VLVVGVLNFF
VV


Related products :

Catalog number Product name Quantity
AS14 2786 rabbit polyclonal PsbN | Potosystem II reaction center protein N 50
AS07 274 Ycf 4 | photosystem I assembly protein ycf4 200 ul
AS07274 Ycf 4 | photosystem I assembly protein ycf4 200 ul
20312228-1 PsaA | PSI-A core protein of photosystem 200 uL
20312295-1 Ycf4 | photosystem I assembly protein yc 200 uL
20312294-1 Ycf3 | Photosystem I assembly protein yc 200 uL
AS06172 PsaA | PSI_A core protein of photosystem I 200 ul
AS03 025 PsaA| PSI_A core protein of photosystem I 400 ug
AS03025 PsaA| PSI_A core protein of photosystem I 400 ug
AS06 172 PsaA | PSI_A core protein of photosystem I 200 ul
AS06 146 PsbD | D2 protein of PSII 100 ul
AS05 059 PsbR | 10 kDa protein of PSII 100 ul
20312152-1 PsbS | 22 kDa Lhc-like PSII protein (hen 100 uL
AS06171 PsbTn | Tn protein of PSII
20312372-1 PsbS | 22 kDa Lhc-like PSII protein (rab 200 uL
AS05059 PsbR | 10 kDa protein of PSII 100 ul
AS06146 PsbD | D2 protein of PSII 100 ul
AS06146 PsbD | D2 protein of PSII 100 µl
20312122-1 PsbD- D2 protein of PSII 100 uL
AS06 172-100 rabbit polyclonal PsaA | PSI-A core protein of photosystem I 2 x 50
AS06 172 rabbit polyclonal PsaA | PSI-A core protein of photosystem I 50
AS09 146S PsbD | D2 protein of PSII protein standard 250 ul
AS06 110 PsbC | CP43 protein of PSII 150 ul
20312178-1 PsbA | D1 protein of PSII, C-terminal (r 10 uL
AS04038 PsbB | CP47 protein of PSII 50 ul


 

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