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

Long chain base biosynthesis protein 1 (AtLCB1) (EC 2.3.1.50) (Protein EMBRYO DEFECTIVE 2779) (Protein FUMONISIN B1 RESISTANT 11)

 LCB1_ARATH              Reviewed;         482 AA.
Q94IB8; B9DHA0; O23233;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 118.
RecName: Full=Long chain base biosynthesis protein 1;
Short=AtLCB1;
EC=2.3.1.50;
AltName: Full=Protein EMBRYO DEFECTIVE 2779;
AltName: Full=Protein FUMONISIN B1 RESISTANT 11;
Name=LCB1; Synonyms=EMB2779, FBR11; OrderedLocusNames=At4g36480;
ORFNames=AP22, C7A10.880;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Mori J., Tamura K., Nishiura H., Morimoto Y., Imai H.;
"Cloning and characterization of a cDNA encoding a subunit of serine
palmitoyltransferase.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9461215; DOI=10.1038/35140;
Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L.,
Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P.,
Wedler H., Wedler E., Wambutt R., Weitzenegger T., Pohl T., Terryn N.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A.,
Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S.,
Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B.,
Mueller-Auer S., Silvey M., James R., Monfort A., Pons A.,
Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P.,
Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T.,
Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W.,
Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W.,
Klosterman S., Schueller C., Chalwatzis N.;
"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of
Arabidopsis thaliana.";
Nature 391:485-488(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia; TISSUE=Rosette leaf;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[7]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, AND SUBUNIT.
PubMed=17194770; DOI=10.1105/tpc.105.040774;
Chen M., Han G., Dietrich C.R., Dunn T.M., Cahoon E.B.;
"The essential nature of sphingolipids in plants as revealed by the
functional identification and characterization of the Arabidopsis LCB1
subunit of serine palmitoyltransferase.";
Plant Cell 18:3576-3593(2006).
[8]
FUNCTION.
PubMed=18059378; DOI=10.1038/cr.2007.100;
Shi L., Bielawski J., Mu J., Dong H., Teng C., Zhang J., Yang X.,
Tomishige N., Hanada K., Hannun Y.A., Zuo J.;
"Involvement of sphingoid bases in mediating reactive oxygen
intermediate production and programmed cell death in Arabidopsis.";
Cell Res. 17:1030-1040(2007).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18218968; DOI=10.1104/pp.107.113506;
Teng C., Dong H., Shi L., Deng Y., Mu J., Zhang J., Yang X., Zuo J.;
"Serine palmitoyltransferase, a key enzyme for de novo synthesis of
sphingolipids, is essential for male gametophyte development in
Arabidopsis.";
Plant Physiol. 146:1322-1332(2008).
-!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer
formed with LCB2 constitutes the catalytic core. Involved in the
regulation of the programmed cell death (PCD) signaling pathway.
Plays an important role during male gametogenesis and
embryogenesis. {ECO:0000269|PubMed:17194770,
ECO:0000269|PubMed:18059378, ECO:0000269|PubMed:18218968}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-
sphinganine + CO(2).
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
-!- SUBUNIT: Heterodimer with LCB2 (LCB2a or LCB2b). Component of the
serine palmitoyltransferase (SPT) complex, composed of LCB1 and
LCB2 (LCB2a or LCB2b). {ECO:0000269|PubMed:17194770}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:17194770}; Single-pass membrane protein
{ECO:0000269|PubMed:17194770}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:17194770}.
-!- DISRUPTION PHENOTYPE: Defective Embryo and pollen lethality. RNAi
mutants display plant size reduction, altered leaf morphology and
increases in relative amounts of saturated sphingolipid long-chain
bases. {ECO:0000269|PubMed:17194770, ECO:0000269|PubMed:18218968}.
-!- MISCELLANEOUS: The fbr11-1 mutant is incapable of initiating
programmed cell death (PCD) after induction by fumonisin B1 (FB1),
a specific inhibitor of ceramide synthase.
-!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB16844.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB80314.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB063254; BAB60898.1; -; mRNA.
EMBL; Z99708; CAB16844.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161589; CAB80314.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE86660.1; -; Genomic_DNA.
EMBL; CP002687; AEE86661.1; -; Genomic_DNA.
EMBL; AY120759; AAM53317.1; -; mRNA.
EMBL; BT000131; AAN15450.1; -; mRNA.
EMBL; AK317450; BAH20117.1; -; mRNA.
PIR; F85430; F85430.
RefSeq; NP_001031796.1; NM_001036719.2.
RefSeq; NP_568005.1; NM_119811.3.
UniGene; At.22137; -.
ProteinModelPortal; Q94IB8; -.
SMR; Q94IB8; -.
BioGrid; 15082; 6.
IntAct; Q94IB8; 2.
STRING; 3702.AT4G36480.1; -.
PaxDb; Q94IB8; -.
PRIDE; Q94IB8; -.
EnsemblPlants; AT4G36480.1; AT4G36480.1; AT4G36480.
EnsemblPlants; AT4G36480.2; AT4G36480.2; AT4G36480.
GeneID; 829800; -.
Gramene; AT4G36480.1; AT4G36480.1; AT4G36480.
Gramene; AT4G36480.2; AT4G36480.2; AT4G36480.
KEGG; ath:AT4G36480; -.
Araport; AT4G36480; -.
TAIR; locus:2115350; AT4G36480.
eggNOG; KOG1358; Eukaryota.
eggNOG; COG0156; LUCA.
HOGENOM; HOG000216602; -.
InParanoid; Q94IB8; -.
KO; K00654; -.
OMA; LGTEGCI; -.
OrthoDB; EOG0936091M; -.
PhylomeDB; Q94IB8; -.
BioCyc; ARA:AT4G36480-MONOMER; -.
BioCyc; MetaCyc:AT4G36480-MONOMER; -.
UniPathway; UPA00222; -.
PRO; PR:Q94IB8; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q94IB8; baseline and differential.
Genevisible; Q94IB8; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0004758; F:serine C-palmitoyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
GO; GO:0043067; P:regulation of programmed cell death; IMP:UniProtKB.
GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:TAIR.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
Acyltransferase; Apoptosis; Complete proteome; Endoplasmic reticulum;
Lipid metabolism; Membrane; Pyridoxal phosphate; Reference proteome;
Sphingolipid metabolism; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 482 Long chain base biosynthesis protein 1.
/FTId=PRO_0000419144.
TRANSMEM 32 52 Helical. {ECO:0000255}.
CONFLICT 306 306 K -> E (in Ref. 6; BAH20117).
{ECO:0000305}.
SEQUENCE 482 AA; 53141 MW; CE23247C3F7ADE28 CRC64;
MASNLVEMFN AALNWVTMIL ESPSARVVLF GVPIRGHFFV EGLLGVVIII LLTRKSYKPP
KRPLTEQEID ELCDEWVPEP LIPPITEDMK HEPPVLESAA GPHTTVNGKD VVNFASANYL
GLIGHEKLLE SCTSALEKYG VGSCGPRGFY GTIDVHLDCE TRISKFLGTP DSILYSYGLS
TMFSTIPCFC KKGDVIVADE GVHWGIQNGL QLSRSTIVYF KHNDMESLRI TLEKIMTKYK
RSKNLRRYIV AEAVYQNSGQ IAPLDEIVKL KEKYRFRVIL DESNSFGVLG RSGRGLAEHH
SVPIEKIDVV TAAMGHALAT EGGFCTGNAR IIDYQRLSSS GYVFSASLPP YLASAAITAI
DVIDQNPDML VKLKQNVALL WKGLSDIKGM SLTSNRESPI VFLKLEKSSG SAKDDLLLLE
KMADRALKED SLLVVSSKRS FLDKCRLPVG IKLYVSAGHS ESDLLKASES LKRLASELLL
KS


Related products :

Catalog number Product name Quantity
EIAAB39767 Homo sapiens,Human,KIAA0526,LCB 2,LCB2,LCB2a,Long chain base biosynthesis protein 2,Long chain base biosynthesis protein 2a,Serine palmitoyltransferase 2,Serine-palmitoyl-CoA transferase 2,SPT 2,SPTLC
EIAAB39768 C20orf38,Homo sapiens,Human,LCB 3,LCB2b,Long chain base biosynthesis protein 2b,Long chain base biosynthesis protein 3,Serine palmitoyltransferase 3,Serine-palmitoyl-CoA transferase 3,SPT 3,SPTLC2L,SP
EIAAB39769 LCB 3,LCB2b,Long chain base biosynthesis protein 2b,Long chain base biosynthesis protein 3,Mouse,Mus musculus,Serine palmitoyltransferase 3,Serine-palmitoyl-CoA transferase 3,SPT 3,Sptlc2l,Sptlc3
EIAAB39766 LCB 2,Lcb2,LCB2a,Long chain base biosynthesis protein 2,Long chain base biosynthesis protein 2a,Mouse,Mus musculus,Serine palmitoyltransferase 2,Serine-palmitoyl-CoA transferase 2,SPT 2,Sptlc2
EIAAB39764 Bos taurus,Bovine,LCB 1,Long chain base biosynthesis protein 1,Serine palmitoyltransferase 1,Serine-palmitoyl-CoA transferase 1,SPT 1,SPT1,SPTLC1
EIAAB39765 LCB 1,Lcb1,Long chain base biosynthesis protein 1,Mouse,Mus musculus,Serine palmitoyltransferase 1,Serine-palmitoyl-CoA transferase 1,SPT 1,SPT1,Sptlc1
EIAAB39763 Homo sapiens,Human,LCB 1,LCB1,Long chain base biosynthesis protein 1,Serine palmitoyltransferase 1,Serine-palmitoyl-CoA transferase 1,SPT 1,SPT1,SPTLC1
EIAAB36854 ACSVL3,FATP3,FATP-3,Fatty acid transport protein 3,Homo sapiens,Human,Long-chain fatty acid transport protein 3,PSEC0067,SLC27A3,Solute carrier family 27 member 3,UNQ367_PRO703,Very long-chain acyl-Co
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB36860 ACSVL2,FACVL2,FATP1,FATP-6,Fatty acid transport protein 6,Fatty-acid-coenzyme A ligase, very long-chain 2,Homo sapiens,Human,hVLCS-H1,Long-chain fatty acid transport protein 6,SLC27A6,Solute carrier f
26-333 SPTLC2 is a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It catalyzes 0.05 mg
EIAAB11760 Diphthamide biosynthesis protein 1,Diphthamide biosynthesis protein 2 homolog-like 1,Diphthamide biosynthesis protein 2-like,DPH1,DPH1 homolog,DPH2L,DPH2L1,DPH2-like 1,DPH-like 1,Homo sapiens,HsDph1,H
EIAAB10624 DCN1-like protein 4,DCUN1 domain-containing protein 4,Dcun1d4,Defective in cullin neddylation protein 1-like protein 4,Mouse,Mus musculus
EIAAB10623 DCN1-like protein 3,DCUN1 domain-containing protein 3,Dcun1d3,Defective in cullin neddylation protein 1-like protein 3,Mouse,Mus musculus
EIAAB10621 Bos taurus,Bovine,DCN1-like protein 3,DCUN1 domain-containing protein 3,DCUN1D3,Defective in cullin neddylation protein 1-like protein 3
EIAAB10620 DCN1-like protein 3,DCUN1 domain-containing protein 3,Dcun1d3,Defective in cullin neddylation protein 1-like protein 3,Rat,Rattus norvegicus
EIAAB10626 Bos taurus,Bovine,DCN1-like protein 5,DCUN1 domain-containing protein 5,DCUN1D5,Defective in cullin neddylation protein 1-like protein 5
EIAAB10627 DCN1-like protein 5,DCUN1 domain-containing protein 5,Dcun1d5,Defective in cullin neddylation protein 1-like protein 5,Mouse,Mus musculus
EIAAB10628 DCN1-like protein 5,DCUN1 domain-containing protein 5,Dcun1d5,Defective in cullin neddylation protein 1-like protein 5,Rat,Rattus norvegicus
EIAAB10629 DCN1-like protein 5,DCUN1 domain-containing protein 5,DCUN1D5,Defective in cullin neddylation protein 1-like protein 5,Homo sapiens,Human
EIAAB10622 DCN1-like protein 3,DCUN1 domain-containing protein 3,DCUN1D3,Defective in cullin neddylation protein 1-like protein 3,Homo sapiens,Human
EIAAB10619 DCN1-like protein 2,DCUN1 domain-containing protein 2,Dcun1d2,Dcun1l2,Defective in cullin neddylation protein 1-like protein 2,Mouse,Mus musculus
EIAAB10625 DCN1-like protein 4,DCUN1 domain-containing protein 4,DCUN1D4,Defective in cullin neddylation protein 1-like protein 4,Homo sapiens,Human,KIAA0276
CSB-EL014703MO Mouse Molybdenum cofactor biosynthesis protein 1 [Includes Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit SpeciesMouse 96T
CSB-EL014703HU Human Molybdenum cofactor biosynthesis protein 1 [Includes Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) 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 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