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

Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 6.4.1.2)

 ACCD_ECOLI              Reviewed;         304 AA.
P0A9Q5; P08193; P76937; P78251;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
22-NOV-2017, entry version 104.
RecName: Full=Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
Short=ACCase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
Short=Acetyl-CoA carboxylase carboxyltransferase subunit beta {ECO:0000255|HAMAP-Rule:MF_01395};
EC=6.4.1.2 {ECO:0000255|HAMAP-Rule:MF_01395};
Name=accD {ECO:0000255|HAMAP-Rule:MF_01395}; Synonyms=dedB, usg;
OrderedLocusNames=b2316, JW2313;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3040739;
Bognar A.L., Osborne C., Shane B.;
"Primary structure of the Escherichia coli folC gene and its
folylpolyglutamate synthetase-dihydrofolate synthetase product and
regulation of expression by an upstream gene.";
J. Biol. Chem. 262:12337-12343(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3040734;
Nonet M.L., Marvel C.C., Tolan D.R.;
"The hisT-purF region of the Escherichia coli K-12 chromosome.
Identification of additional genes of the hisT and purF operons.";
J. Biol. Chem. 262:12209-12217(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[4]
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).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
PubMed=7678242; DOI=10.1128/jb.175.2.332-340.1993;
Li S.-J., Cronan J.E. Jr.;
"Growth rate regulation of Escherichia coli acetyl coenzyme A
carboxylase, which catalyzes the first committed step of lipid
biosynthesis.";
J. Bacteriol. 175:332-340(1993).
[7]
SIMILARITY TO ZFPA.
PubMed=1886618; DOI=10.1007/BF00282448;
Nagano Y., Matsuno R., Sasaki Y.;
"An essential gene of Escherichia coli that has sequence similarity to
a chloroplast gene of unknown function.";
Mol. Gen. Genet. 228:62-64(1991).
[8]
FUNCTION.
PubMed=1355086; DOI=10.1128/jb.174.17.5755-5757.1992;
Li S.-J., Rock C.O., Cronan J.E. Jr.;
"The dedB (usg) open reading frame of Escherichia coli encodes a
subunit of acetyl-coenzyme A carboxylase.";
J. Bacteriol. 174:5755-5757(1992).
[9]
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=15066985; DOI=10.1074/jbc.M402989200;
Freiberg C., Brunner N.A., Schiffer G., Lampe T., Pohlmann J.,
Brands M., Raabe M., Haebich D., Ziegelbauer K.;
"Identification and characterization of the first class of potent
bacterial acetyl-CoA carboxylase inhibitors with antibacterial
activity.";
J. Biol. Chem. 279:26066-26073(2004).
[10]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RNA-BINDING,
SUGGESTED MECHANISM OF TRANSLATIONAL REGULATION, AND MUTAGENESIS OF
CYS-27; CYS-30; CYS-46 AND CYS-49.
PubMed=19965770; DOI=10.1093/nar/gkp1079;
Meades G. Jr., Benson B.K., Grove A., Waldrop G.L.;
"A tale of two functions: enzymatic activity and translational
repression by carboxyltransferase.";
Nucleic Acids Res. 38:1217-1227(2010).
[11]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), AND ZINC-FINGER.
PubMed=16460018; DOI=10.1021/bi0520479;
Bilder P., Lightle S., Bainbridge G., Ohren J., Finzel B., Sun F.,
Holley S., Al-Kassim L., Spessard C., Melnick M., Newcomer M.,
Waldrop G.L.;
"The structure of the carboxyltransferase component of acetyl-coA
carboxylase reveals a zinc-binding motif unique to the bacterial
enzyme.";
Biochemistry 45:1712-1722(2006).
-!- FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC)
complex. Biotin carboxylase (BC) catalyzes the carboxylation of
biotin on its carrier protein (BCCP) and then the CO(2) group is
transferred by the transcarboxylase to acetyl-CoA to form malonyl-
CoA.
-!- FUNCTION: Controls translation of mRNA for both itself and the
alpha-subunit (accA) by binding to a probable hairpin in the 5' of
the mRNA. Binding to mRNA inhibits translation; this is partially
relieved by acetyl-CoA. Increasing amounts of mRNA also inhibit
enzyme activity.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01395}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_01395,
ECO:0000269|PubMed:19965770};
Note=Binds 1 zinc ion per subunit. The zinc is involved in both
translation regulation via mRNA-binding and catalysis.
{ECO:0000255|HAMAP-Rule:MF_01395, ECO:0000269|PubMed:19965770};
-!- ENZYME REGULATION: Competitively inhibited by pyrrolidine dione
antibiotic moiramide B (CPD1). {ECO:0000269|PubMed:15066985}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=40.0 uM for malonyl-CoA {ECO:0000269|PubMed:15066985,
ECO:0000269|PubMed:19965770};
KM=11.4 mM for biocytin {ECO:0000269|PubMed:15066985,
ECO:0000269|PubMed:19965770};
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01395}.
-!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC)
and two subunits each of ACCase subunit alpha (AccA) and ACCase
subunit beta (AccD).
-!- INTERACTION:
P0ABD5:accA; NbExp=17; IntAct=EBI-542064, EBI-542031;
P24182:accC; NbExp=4; IntAct=EBI-542064, EBI-542308;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000255|HAMAP-
Rule:MF_01395}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M32445; AAA23807.1; -; Genomic_DNA.
EMBL; J02808; AAA23801.1; -; Genomic_DNA.
EMBL; M68934; AAA23965.1; -; Genomic_DNA.
EMBL; U00096; AAC75376.1; -; Genomic_DNA.
EMBL; AP009048; BAA16173.1; -; Genomic_DNA.
EMBL; S53037; AAB24894.2; -; mRNA.
PIR; B65004; XMECBD.
RefSeq; NP_416819.1; NC_000913.3.
RefSeq; WP_000118404.1; NZ_LN832404.1.
PDB; 2F9Y; X-ray; 3.20 A; B=1-304.
PDBsum; 2F9Y; -.
ProteinModelPortal; P0A9Q5; -.
SMR; P0A9Q5; -.
BioGrid; 4261361; 233.
DIP; DIP-35878N; -.
IntAct; P0A9Q5; 28.
MINT; MINT-1234646; -.
STRING; 316385.ECDH10B_2478; -.
PaxDb; P0A9Q5; -.
PRIDE; P0A9Q5; -.
EnsemblBacteria; AAC75376; AAC75376; b2316.
EnsemblBacteria; BAA16173; BAA16173; BAA16173.
GeneID; 946796; -.
KEGG; ecj:JW2313; -.
KEGG; eco:b2316; -.
PATRIC; fig|511145.12.peg.2411; -.
EchoBASE; EB0213; -.
EcoGene; EG10217; accD.
eggNOG; ENOG4108IDZ; Bacteria.
eggNOG; COG0777; LUCA.
HOGENOM; HOG000021670; -.
InParanoid; P0A9Q5; -.
KO; K01963; -.
PhylomeDB; P0A9Q5; -.
BioCyc; EcoCyc:CARBOXYL-TRANSFERASE-BETA-MONOMER; -.
BioCyc; MetaCyc:CARBOXYL-TRANSFERASE-BETA-MONOMER; -.
SABIO-RK; P0A9Q5; -.
UniPathway; UPA00655; UER00711.
EvolutionaryTrace; P0A9Q5; -.
PRO; PR:P0A9Q5; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009329; C:acetate CoA-transferase complex; IDA:EcoCyc.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:EcoliWiki.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IMP:EcoCyc.
GO; GO:0003729; F:mRNA binding; IDA:EcoCyc.
GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
GO; GO:0006633; P:fatty acid biosynthetic process; IMP:EcoCyc.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; NAS:EcoliWiki.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0017148; P:negative regulation of translation; IDA:EcoCyc.
HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011762; COA_CT_N.
Pfam; PF01039; Carboxyl_trans; 1.
PRINTS; PR01070; ACCCTRFRASEB.
SUPFAM; SSF52096; SSF52096; 1.
TIGRFAMs; TIGR00515; accD; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
Lipid biosynthesis; Lipid metabolism; Metal-binding;
Nucleotide-binding; Reference proteome; RNA-binding;
Translation regulation; Zinc; Zinc-finger.
CHAIN 1 304 Acetyl-coenzyme A carboxylase carboxyl
transferase subunit beta.
/FTId=PRO_0000199770.
DOMAIN 23 292 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
ZN_FING 27 49 C4-type. {ECO:0000305}.
METAL 27 27 Zinc.
METAL 30 30 Zinc.
METAL 46 46 Zinc.
METAL 49 49 Zinc.
MUTAGEN 27 27 C->A: Vmax decreases 9-fold.
{ECO:0000269|PubMed:19965770}.
MUTAGEN 30 30 C->A: Vmax decreases 140-fold. Loss of
nucleic acid-binding.
{ECO:0000269|PubMed:19965770}.
MUTAGEN 46 46 C->A: Vmax decreases 11-fold.
{ECO:0000269|PubMed:19965770}.
MUTAGEN 49 49 C->A: Vmax decreases 8-fold.
{ECO:0000269|PubMed:19965770}.
CONFLICT 76 77 EL -> SV (in Ref. 2; AAA23965).
{ECO:0000305}.
CONFLICT 225 239 IGFAGPRVIEQTVRE -> MALPVRVLSNRPFAK (in
Ref. 1; AAA23807/AAA23801).
{ECO:0000305}.
CONFLICT 226 235 GFAGPRVIEQ -> ALPVRVLSNR (in Ref. 2;
AAA23965). {ECO:0000305}.
TURN 28 30 {ECO:0000244|PDB:2F9Y}.
TURN 36 44 {ECO:0000244|PDB:2F9Y}.
TURN 47 49 {ECO:0000244|PDB:2F9Y}.
HELIX 57 64 {ECO:0000244|PDB:2F9Y}.
HELIX 88 90 {ECO:0000244|PDB:2F9Y}.
STRAND 105 112 {ECO:0000244|PDB:2F9Y}.
STRAND 121 125 {ECO:0000244|PDB:2F9Y}.
TURN 130 132 {ECO:0000244|PDB:2F9Y}.
HELIX 137 152 {ECO:0000244|PDB:2F9Y}.
STRAND 156 165 {ECO:0000244|PDB:2F9Y}.
HELIX 167 170 {ECO:0000244|PDB:2F9Y}.
HELIX 171 189 {ECO:0000244|PDB:2F9Y}.
STRAND 194 203 {ECO:0000244|PDB:2F9Y}.
HELIX 204 207 {ECO:0000244|PDB:2F9Y}.
HELIX 210 212 {ECO:0000244|PDB:2F9Y}.
STRAND 215 219 {ECO:0000244|PDB:2F9Y}.
STRAND 224 228 {ECO:0000244|PDB:2F9Y}.
HELIX 230 237 {ECO:0000244|PDB:2F9Y}.
TURN 243 246 {ECO:0000244|PDB:2F9Y}.
HELIX 248 251 {ECO:0000244|PDB:2F9Y}.
HELIX 252 254 {ECO:0000244|PDB:2F9Y}.
STRAND 258 260 {ECO:0000244|PDB:2F9Y}.
HELIX 263 277 {ECO:0000244|PDB:2F9Y}.
SEQUENCE 304 AA; 33322 MW; 401FEC94D728F3CB CRC64;
MSWIERIKSN ITPTRKASIP EGVWTKCDSC GQVLYRAELE RNLEVCPKCD HHMRMTARNR
LHSLLDEGSL VELGSELEPK DVLKFRDSKK YKDRLASAQK ETGEKDALVV MKGTLYGMPV
VAAAFEFAFM GGSMGSVVGA RFVRAVEQAL EDNCPLICFS ASGGARMQEA LMSLMQMAKT
SAALAKMQER GLPYISVLTD PTMGGVSASF AMLGDLNIAE PKALIGFAGP RVIEQTVREK
LPPGFQRSEF LIEKGAIDMI VRRPEMRLKL ASILAKLMNL PAPNPEAPRE GVVVPPVPDQ
EPEA


Related products :

Catalog number Product name Quantity
EIAAB30046 PCCase subunit beta,PCCB,Pig,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial,Sus scrofa
EIAAB30047 Mouse,Mus musculus,PCCase subunit beta,Pccb,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
EIAAB30045 Bos taurus,Bovine,PCCase subunit beta,PCCB,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
EIAAB30044 PCCase subunit beta,Pccb,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial,Rat,Rattus norvegicus
EIAAB30043 Homo sapiens,Human,PCCase subunit beta,PCCB,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
E0195h ELISA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,HEXA,Hexosaminidase subunit A,Homo sapiens,Human,N-acetyl-beta-glucosaminidase subunit alpha 96T
U0195h CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,HEXA,Hexosaminidase subunit A,Homo sapiens,Human,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195h ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,HEXA,Hexosaminidase subunit A,Homo sapiens,Human,N-acetyl-beta-glucosaminidase subunit alpha 96T
U0195r CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha,Rat,Rattus norvegicus 96T
U0195b CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Bos taurus,Bovine,HEXA,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195m ELISA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,Mouse,Mus musculus,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195b ELISA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Bos taurus,Bovine,HEXA,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha 96T
U0195m CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,Mouse,Mus musculus,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195r ELISA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha,Rat,Rattus norvegicus 96T
E0195b ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Bos taurus,Bovine,HEXA,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195m ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,Mouse,Mus musculus,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195r ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha,Rat,Rattus norvegicus 96T
EIAAB30800 Geranylgeranyl transferase type II subunit beta,Geranylgeranyl transferase type-2 subunit beta,GGTase-II-beta,Ggtb,Rab geranylgeranyltransferase subunit beta,Rab geranyl-geranyltransferase subunit bet
EIAAB30799 Geranylgeranyl transferase type II subunit beta,Geranylgeranyl transferase type-2 subunit beta,GGTase-II-beta,GGTB,Homo sapiens,Human,Rab geranylgeranyltransferase subunit beta,Rab geranyl-geranyltran
E10431h Human Acetyl Coenzyme A Carboxylase Beta ELISA Kit 96T
EIAAB30798 Bos taurus,Bovine,Geranylgeranyl transferase type II subunit beta,Geranylgeranyl transferase type-2 subunit beta,GGTase-II-beta,Rab geranylgeranyltransferase subunit beta,Rab geranyl-geranyltransferas
EIAAB30797 Geranylgeranyl transferase type II subunit beta,Geranylgeranyl transferase type-2 subunit beta,GGTase-II-beta,Mouse,Mus musculus,Rab geranylgeranyltransferase subunit beta,Rab geranyl-geranyltransfera
EIAAB30795 Geranylgeranyl transferase type I subunit beta,Geranylgeranyl transferase type-1 subunit beta,GGTase-I-beta,Homo sapiens,Human,PGGT1B,Type I protein geranyl-geranyltransferase subunit beta
EIAAB30796 Geranylgeranyl transferase type I subunit beta,Geranylgeranyl transferase type-1 subunit beta,GGTase-I-beta,Pggt1b,Rat,Rattus norvegicus,Type I protein geranyl-geranyltransferase subunit beta
EIAAB30793 Bos taurus,Bovine,Geranylgeranyl transferase type I subunit beta,Geranylgeranyl transferase type-1 subunit beta,GGTase-I-beta,PGGT1B,Type I protein geranyl-geranyltransferase subunit beta


 

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