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

Peroxisomal multifunctional enzyme type 2 (DmMFE-2) [Includes: (3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12); Enoyl-CoA hydratase 2 (EC 4.2.1.119)]

 DHB4_DROME              Reviewed;         598 AA.
Q9VXJ0;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 149.
RecName: Full=Peroxisomal multifunctional enzyme type 2 {ECO:0000303|PubMed:21320074};
Short=DmMFE-2 {ECO:0000303|PubMed:21320074};
Includes:
RecName: Full=(3R)-hydroxyacyl-CoA dehydrogenase {ECO:0000303|PubMed:21320074};
EC=1.1.1.n12 {ECO:0000269|PubMed:21320074};
Includes:
RecName: Full=Enoyl-CoA hydratase 2 {ECO:0000303|PubMed:21320074};
EC=4.2.1.119 {ECO:0000269|PubMed:21320074};
Name=Mfe2 {ECO:0000312|FlyBase:FBgn0030731}; ORFNames=CG3415;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000312|EMBL:AAF48572.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF48572.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3] {ECO:0000312|EMBL:AAK92917.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Head {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4] {ECO:0000305, ECO:0000312|PDB:3OML}
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=21320074; DOI=10.1042/BJ20101661;
Haataja T.J., Koski M.K., Hiltunen J.K., Glumoff T.;
"Peroxisomal multifunctional enzyme type 2 from the fruitfly:
dehydrogenase and hydratase act as separate entities, as revealed by
structure and kinetics.";
Biochem. J. 435:771-781(2011).
-!- FUNCTION: Bifunctional enzyme acting on the peroxisomal beta-
oxidation pathway for fatty acids. {ECO:0000269|PubMed:21320074}.
-!- CATALYTIC ACTIVITY: (R)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH. {ECO:0000269|PubMed:21320074}.
-!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA +
H(2)O. {ECO:0000269|PubMed:21320074}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=85.3 uM for (2E)-butenoyl-CoA (at 22 degrees Celsius)
{ECO:0000269|PubMed:21320074};
KM=66.7 uM for (2E)-hexenoyl-CoA (at 22 degrees Celsius)
{ECO:0000269|PubMed:21320074};
KM=31.4 uM for (2E)-decenoyl-CoA (at 22 degrees Celsius)
{ECO:0000269|PubMed:21320074};
Vmax=1.07 umol/min/mg enzyme with (2E)-butenoyl-CoA (at 22
degrees Celsius) {ECO:0000269|PubMed:21320074};
Vmax=15.0 umol/min/mg enzyme with (2E)-hexenoyl-CoA (at 22
degrees Celsius) {ECO:0000269|PubMed:21320074};
Vmax=31.4 umol/min/mg enzyme with (2E)-decenoyl-CoA (at 22
degrees Celsius) {ECO:0000269|PubMed:21320074};
Note=Catalytic efficiency is similar using full-length protein
or the individual (3R)-hydroxyacyl-CoA dehydrogenase and enoyl-
CoA hydratase 2 domains in a 1:1 mixture.
{ECO:0000269|PubMed:21320074};
-!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
{ECO:0000250|UniProtKB:P51659}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21320074}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P51659}.
-!- MISCELLANEOUS: Complements functionally the S.cerevisiae
peroxisomal MFE-2 in vivo.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000255}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AE014298; AAF48572.1; -; Genomic_DNA.
EMBL; AY051493; AAK92917.1; -; mRNA.
RefSeq; NP_001285318.1; NM_001298389.1.
RefSeq; NP_573109.1; NM_132881.3.
UniGene; Dm.4585; -.
PDB; 3OML; X-ray; 2.15 A; A=1-598.
PDBsum; 3OML; -.
ProteinModelPortal; Q9VXJ0; -.
SMR; Q9VXJ0; -.
BioGrid; 58924; 10.
IntAct; Q9VXJ0; 4.
MINT; Q9VXJ0; -.
STRING; 7227.FBpp0073988; -.
PaxDb; Q9VXJ0; -.
PRIDE; Q9VXJ0; -.
EnsemblMetazoa; FBtr0074209; FBpp0073988; FBgn0030731.
EnsemblMetazoa; FBtr0340442; FBpp0309384; FBgn0030731.
GeneID; 32582; -.
KEGG; dme:Dmel_CG3415; -.
UCSC; CG3415-RA; d. melanogaster.
CTD; 32582; -.
FlyBase; FBgn0030731; Mfe2.
eggNOG; KOG1206; Eukaryota.
eggNOG; COG2030; LUCA.
InParanoid; Q9VXJ0; -.
KO; K12405; -.
OMA; SRMTQTV; -.
OrthoDB; EOG091G02S9; -.
PhylomeDB; Q9VXJ0; -.
Reactome; R-DME-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-DME-2046106; alpha-linolenic acid (ALA) metabolism.
Reactome; R-DME-389887; Beta-oxidation of pristanoyl-CoA.
Reactome; R-DME-390247; Beta-oxidation of very long chain fatty acids.
Reactome; R-DME-9033241; Peroxisomal protein import.
UniPathway; UPA00659; -.
EvolutionaryTrace; Q9VXJ0; -.
GenomeRNAi; 32582; -.
PRO; PR:Q9VXJ0; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0030731; -.
ExpressionAtlas; Q9VXJ0; baseline and differential.
Genevisible; Q9VXJ0; DM.
GO; GO:0005777; C:peroxisome; ISS:FlyBase.
GO; GO:0080023; F:3R-hydroxyacyl-CoA dehydratase activity; IDA:FlyBase.
GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:FlyBase.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IC:FlyBase.
InterPro; IPR029069; HotDog_dom_sf.
InterPro; IPR002539; MaoC_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
Pfam; PF01575; MaoC_dehydratas; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF54637; SSF54637; 2.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Fatty acid metabolism;
Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase;
Peroxisome; Reference proteome.
CHAIN 1 598 Peroxisomal multifunctional enzyme type
2.
/FTId=PRO_0000416935.
DOMAIN 469 586 MaoC-like. {ECO:0000255}.
NP_BIND 16 40 NAD. {ECO:0000250|UniProtKB:P51659}.
NP_BIND 78 79 NAD. {ECO:0000250|UniProtKB:P51659}.
NP_BIND 167 171 NAD. {ECO:0000250|UniProtKB:P51659}.
NP_BIND 199 202 NAD. {ECO:0000250|UniProtKB:P51659}.
REGION 1 309 (3R)-hydroxyacyl-CoA dehydrogenase.
{ECO:0000269|PubMed:21320074}.
REGION 310 598 Enoyl-CoA hydratase 2.
{ECO:0000269|PubMed:21320074}.
REGION 390 391 (3R)-3-hydroxydecanoyl-CoA binding.
{ECO:0000250|UniProtKB:P22414}.
REGION 496 501 (3R)-3-hydroxydecanoyl-CoA binding.
{ECO:0000250|UniProtKB:P22414}.
MOTIF 596 598 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 167 167 Proton acceptor.
{ECO:0000250|UniProtKB:P51659,
ECO:0000255|PROSITE-ProRule:PRU10001}.
BINDING 24 24 NAD; via amide nitrogen.
{ECO:0000250|UniProtKB:P51659}.
BINDING 43 43 NAD. {ECO:0000250|UniProtKB:P51659}.
BINDING 102 102 NAD; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P51659}.
BINDING 154 154 Substrate.
{ECO:0000250|UniProtKB:P51659}.
BINDING 419 419 (3R)-3-hydroxydecanoyl-CoA.
{ECO:0000250|UniProtKB:P22414}.
BINDING 519 519 (3R)-3-hydroxydecanoyl-CoA; via amide
nitrogen. {ECO:0000250|UniProtKB:P22414}.
BINDING 549 549 (3R)-3-hydroxydecanoyl-CoA; via carbonyl
oxygen. {ECO:0000250|UniProtKB:P22414}.
STRAND 14 17 {ECO:0000244|PDB:3OML}.
TURN 18 21 {ECO:0000244|PDB:3OML}.
HELIX 23 34 {ECO:0000244|PDB:3OML}.
STRAND 38 41 {ECO:0000244|PDB:3OML}.
HELIX 58 67 {ECO:0000244|PDB:3OML}.
STRAND 72 74 {ECO:0000244|PDB:3OML}.
HELIX 79 81 {ECO:0000244|PDB:3OML}.
HELIX 82 86 {ECO:0000244|PDB:3OML}.
HELIX 116 142 {ECO:0000244|PDB:3OML}.
TURN 143 145 {ECO:0000244|PDB:3OML}.
STRAND 147 152 {ECO:0000244|PDB:3OML}.
HELIX 155 159 {ECO:0000244|PDB:3OML}.
HELIX 165 185 {ECO:0000244|PDB:3OML}.
HELIX 186 188 {ECO:0000244|PDB:3OML}.
STRAND 190 197 {ECO:0000244|PDB:3OML}.
HELIX 210 213 {ECO:0000244|PDB:3OML}.
HELIX 218 220 {ECO:0000244|PDB:3OML}.
HELIX 222 227 {ECO:0000244|PDB:3OML}.
STRAND 239 243 {ECO:0000244|PDB:3OML}.
STRAND 246 250 {ECO:0000244|PDB:3OML}.
STRAND 260 263 {ECO:0000244|PDB:3OML}.
HELIX 270 275 {ECO:0000244|PDB:3OML}.
HELIX 277 280 {ECO:0000244|PDB:3OML}.
HELIX 292 307 {ECO:0000244|PDB:3OML}.
STRAND 314 320 {ECO:0000244|PDB:3OML}.
HELIX 322 331 {ECO:0000244|PDB:3OML}.
HELIX 339 341 {ECO:0000244|PDB:3OML}.
HELIX 342 345 {ECO:0000244|PDB:3OML}.
HELIX 356 360 {ECO:0000244|PDB:3OML}.
HELIX 361 369 {ECO:0000244|PDB:3OML}.
STRAND 389 397 {ECO:0000244|PDB:3OML}.
STRAND 403 418 {ECO:0000244|PDB:3OML}.
STRAND 423 432 {ECO:0000244|PDB:3OML}.
STRAND 438 448 {ECO:0000244|PDB:3OML}.
STRAND 476 482 {ECO:0000244|PDB:3OML}.
HELIX 487 491 {ECO:0000244|PDB:3OML}.
HELIX 492 494 {ECO:0000244|PDB:3OML}.
HELIX 499 501 {ECO:0000244|PDB:3OML}.
HELIX 504 509 {ECO:0000244|PDB:3OML}.
HELIX 519 534 {ECO:0000244|PDB:3OML}.
HELIX 539 541 {ECO:0000244|PDB:3OML}.
STRAND 542 549 {ECO:0000244|PDB:3OML}.
STRAND 558 566 {ECO:0000244|PDB:3OML}.
STRAND 569 576 {ECO:0000244|PDB:3OML}.
TURN 577 579 {ECO:0000244|PDB:3OML}.
STRAND 582 591 {ECO:0000244|PDB:3OML}.
SEQUENCE 598 AA; 64073 MW; 24205DE78964319A CRC64;
MSSSDGKLRY DGRVAVVTGA GAGLGREYAL LFAERGAKVV VNDLGGTHSG DGASQRAADI
VVDEIRKAGG EAVADYNSVI DGAKVIETAI KAFGRVDILV NNAGILRDRS LVKTSEQDWN
LVNDVHLKGS FKCTQAAFPY MKKQNYGRII MTSSNSGIYG NFGQVNYTAA KMGLIGLANT
VAIEGARNNV LCNVIVPTAA SRMTEGILPD ILFNELKPKL IAPVVAYLCH ESCEDNGSYI
ESAAGWATKL HMVRGKGAVL RPSLDDPVTI EYVKDVWSNV TDMSKAKHLG AIAEASGTLL
EVLEKLKEGG GDAIEDAFEF NSKELITYAL GIGASVKNAK DMRFLYENDA DFAAIPTFFV
LPGLLLQMST DKLLSKALPN SQVDFSNILH GEQYLEIVDD LPTSGTLLTN GKVFDVMDKG
SGAVVVTNSE SFDESGRLLV RNQSTTFIVG AGKFGGKKDP IAGVVPLQPA PNRQPDATVQ
YTTSEDQAAL YRLSGDKNPL HIDPQMALLA GFKTPILHGL CTLGFSVRAV LAQFADNNPA
LFKAVKVRFS GPVIPGQTLR VDLWKQGTRI NFRTVVVETG KEVISGAYVD LKSSQAKL


Related products :

Catalog number Product name Quantity
EIAAB11111 17-beta-HSD 4,17-beta-hydroxysteroid dehydrogenase 4,D-bifunctional protein,DBP,Edh17b4,Hsd17b4,MFE-2,Mouse,MPF-2,Multifunctional protein 2,Mus musculus,Peroxisomal multifunctional enzyme type 2
EIAAB11110 17-beta-HSD 4,17-beta-hydroxysteroid dehydrogenase 4,D-bifunctional protein,DBP,Edh17b4,Hsd17b4,MFE-2,MPF-2,Multifunctional protein 2,Peroxisomal multifunctional enzyme type 2,Rat,Rattus norvegicus
EIAAB11109 17-beta-HSD 4,17-beta-hydroxysteroid dehydrogenase 4,D-bifunctional protein,DBP,EDH17B4,Homo sapiens,HSD17B4,Human,MFE-2,MPF-2,Multifunctional protein 2,Peroxisomal multifunctional enzyme type 2
EIAAB12372 ECHS1,Enoyl-CoA hydratase 1,Enoyl-CoA hydratase, mitochondrial,Homo sapiens,Human,SCEH,Short-chain enoyl-CoA hydratase
EIAAB12373 Echs1,Enoyl-CoA hydratase 1,Enoyl-CoA hydratase, mitochondrial,Mouse,Mus musculus,SCEH,Short-chain enoyl-CoA hydratase
EIAAB12371 Bos taurus,Bovine,ECHS1,Enoyl-CoA hydratase 1,Enoyl-CoA hydratase, mitochondrial,SCEH,Short-chain enoyl-CoA hydratase
EIAAB12370 Echs1,Enoyl-CoA hydratase 1,Enoyl-CoA hydratase, mitochondrial,Rat,Rattus norvegicus,SCEH,Short-chain enoyl-CoA hydratase
CSB-EL007378RA Rat enoyl Coenzyme A hydratase 1, peroxisomal (ECH1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL010774RA Rat Peroxisomal multifunctional enzyme type 2(HSD17B4) ELISA kit 96T
CSB-EL010774HU Human Peroxisomal multifunctional enzyme type 2(HSD17B4) ELISA kit 96T
CSB-EL010774RA Rat Peroxisomal multifunctional enzyme type 2(HSD17B4) ELISA kit SpeciesRat 96T
CSB-EL010774MO Mouse Peroxisomal multifunctional enzyme type 2(HSD17B4) ELISA kit 96T
enz-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 1mg
REN-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 5
enz-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 20
enz-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 5
CSB-EL010774HU Human Peroxisomal multifunctional enzyme type 2(HSD17B4) ELISA kit SpeciesHuman 96T
CSB-EL010774MO Mouse Peroxisomal multifunctional enzyme type 2(HSD17B4) ELISA kit SpeciesMouse 96T
DHB4_RAT ELISA Kit FOR Peroxisomal multifunctional enzyme type 2; organism: Rat; gene name: Hsd17b4 96T
enz-562 Recombinant Human Enoyl CoA Hydratase 1 Peroxisomal ENZYMES 20
OETENZ-562 Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant 5
enz-562 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal ECH1 20
7-02709 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 1mg
OETENZ-562 Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant 20
7-02708 Recombinant Human Enoyl CoA Hydratase 1, Peroxisomal 20


 

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