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Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase)

 DLDH_MOUSE              Reviewed;         509 AA.
O08749; Q3TG55; Q3U5W5; Q3UWP7; Q99LD3;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 2.
25-OCT-2017, entry version 160.
RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
EC=1.8.1.4 {ECO:0000250|UniProtKB:P09622};
AltName: Full=Dihydrolipoamide dehydrogenase;
Flags: Precursor;
Name=Dld;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=DBA/2J;
PubMed=9169128; DOI=10.1006/geno.1997.4670;
Johnson M., Yang H.S., Johanning G.L., Patel M.S.;
"Characterization of the mouse dihydrolipoamide dehydrogenase (Dld)
gene: genomic structure, promoter sequence, and chromosomal
localization.";
Genomics 41:320-326(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 73-89; 216-259; 289-334; 316-334; 347-365; 421-428
AND 483-509, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
SUBCELLULAR LOCATION.
PubMed=15888450; DOI=10.1074/jbc.M500310200;
Mitra K., Rangaraj N., Shivaji S.;
"Novelty of the pyruvate metabolic enzyme dihydrolipoamide
dehydrogenase in spermatozoa: correlation of its localization,
tyrosine phosphorylation, and activity during sperm capacitation.";
J. Biol. Chem. 280:25743-25753(2005).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17404228; DOI=10.1073/pnas.0610618104;
Babady N.E., Pang Y.P., Elpeleg O., Isaya G.;
"Cryptic proteolytic activity of dihydrolipoamide dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 104:6158-6163(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-410,
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122;
LYS-132; LYS-143; LYS-159; LYS-166; LYS-273; LYS-277; LYS-334;
LYS-410; LYS-430 AND LYS-505, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122;
LYS-132; LYS-143; LYS-334; LYS-346; LYS-410; LYS-420 AND LYS-505, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
cleavage system as well as an E3 component of the alpha-ketoacid
dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and
branched-chain amino acid-dehydrogenase complex). In monomeric
form has additional moonlighting function as serine protease
(PubMed:17404228). Involved in the hyperactivation of spermatazoa
during capacitation and in the spermatazoal acrosome reaction (By
similarity). {ECO:0000250|UniProtKB:Q811C4,
ECO:0000269|PubMed:17404228}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
{ECO:0000250|UniProtKB:P09622}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:P09622};
Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622};
-!- SUBUNIT: Homodimer. Part of the multimeric pyruvate dehydrogenase
complex that contains multiple copies of pyruvate dehydrogenase
(subunits PDH1A and PDHB, E1), dihydrolipoamide acetyltransferase
(DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits
are bound to an inner core composed of about 48 DLAT and 12 PDHX
molecules (by non covalent bonds). Interacts with PDHX.
{ECO:0000250|UniProtKB:P09622}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000305|PubMed:9169128}. Cytoplasmic vesicle, secretory
vesicle, acrosome {ECO:0000269|PubMed:15888450}. Cell projection,
cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}.
-!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
{ECO:0000269|PubMed:17404228}.
-!- PTM: Acetylation of Lys-127 is observed in liver mitochondria from
fasted mice but not from fed mice.
-!- PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
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EMBL; U73445; AAC53170.1; -; mRNA.
EMBL; AK117104; BAE43405.1; -; mRNA.
EMBL; AK136193; BAE22867.1; -; mRNA.
EMBL; AK153399; BAE31961.1; -; mRNA.
EMBL; AK168875; BAE40693.1; -; mRNA.
EMBL; BC003368; AAH03368.1; -; mRNA.
CCDS; CCDS36428.1; -.
RefSeq; NP_031887.2; NM_007861.5.
UniGene; Mm.3131; -.
UniGene; Mm.471230; -.
ProteinModelPortal; O08749; -.
SMR; O08749; -.
BioGrid; 199227; 5.
IntAct; O08749; 11.
MINT; MINT-4124146; -.
STRING; 10090.ENSMUSP00000106481; -.
ChEMBL; CHEMBL2176826; -.
iPTMnet; O08749; -.
PhosphoSitePlus; O08749; -.
SwissPalm; O08749; -.
REPRODUCTION-2DPAGE; O08749; -.
SWISS-2DPAGE; O08749; -.
EPD; O08749; -.
MaxQB; O08749; -.
PaxDb; O08749; -.
PeptideAtlas; O08749; -.
PRIDE; O08749; -.
Ensembl; ENSMUST00000110857; ENSMUSP00000106481; ENSMUSG00000020664.
GeneID; 13382; -.
KEGG; mmu:13382; -.
UCSC; uc007nhg.3; mouse.
CTD; 1738; -.
MGI; MGI:107450; Dld.
eggNOG; KOG1335; Eukaryota.
eggNOG; COG1249; LUCA.
GeneTree; ENSGT00550000074844; -.
HOGENOM; HOG000276708; -.
HOVERGEN; HBG002290; -.
InParanoid; O08749; -.
KO; K00382; -.
OMA; TMSEAVM; -.
OrthoDB; EOG091G05AA; -.
PhylomeDB; O08749; -.
TreeFam; TF300414; -.
Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
Reactome; R-MMU-6783984; Glycine degradation.
Reactome; R-MMU-70268; Pyruvate metabolism.
Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
Reactome; R-MMU-71064; Lysine catabolism.
Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
PRO; PR:O08749; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020664; -.
CleanEx; MM_DLD; -.
Genevisible; O08749; MM.
GO; GO:0043159; C:acrosomal matrix; IDA:MGI.
GO; GO:0005929; C:cilium; IDA:MGI.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
GO; GO:0045254; C:pyruvate dehydrogenase complex; ISO:MGI.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IMP:MGI.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl.
GO; GO:0043544; F:lipoamide binding; IEA:Ensembl.
GO; GO:0051287; F:NAD binding; IEA:Ensembl.
GO; GO:0034604; F:pyruvate dehydrogenase (NAD+) activity; IEA:Ensembl.
GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0051068; P:dihydrolipoamide metabolic process; IEA:Ensembl.
GO; GO:0007369; P:gastrulation; IMP:MGI.
GO; GO:0009106; P:lipoate metabolic process; IEA:Ensembl.
GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; ISO:MGI.
GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:MGI.
GO; GO:0006508; P:proteolysis; IDA:MGI.
GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
GO; GO:0048240; P:sperm capacitation; IDA:MGI.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
Acetylation; Cell projection; Cilium; Complete proteome;
Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; FAD;
Flagellum; Flavoprotein; Mitochondrion; NAD; Oxidoreductase;
Phosphoprotein; Redox-active center; Reference proteome;
Transit peptide.
TRANSIT 1 35 Mitochondrion. {ECO:0000250}.
CHAIN 36 509 Dihydrolipoyl dehydrogenase,
mitochondrial.
/FTId=PRO_0000030297.
NP_BIND 71 80 FAD. {ECO:0000250}.
NP_BIND 183 185 FAD. {ECO:0000250}.
NP_BIND 220 227 NAD. {ECO:0000250}.
NP_BIND 361 364 FAD. {ECO:0000250}.
ACT_SITE 487 487 Proton acceptor. {ECO:0000250}.
BINDING 89 89 FAD. {ECO:0000250}.
BINDING 154 154 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 243 243 NAD. {ECO:0000250}.
BINDING 278 278 NAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 314 314 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 355 355 FAD. {ECO:0000250}.
SITE 448 448 Important for interaction with PDHX and
activity of pyruvate dehydrogenase
complex. {ECO:0000250|UniProtKB:P09622}.
SITE 473 473 Important for interaction with PDHX and
activity of pyruvate dehydrogenase
complex. {ECO:0000250|UniProtKB:P09622}.
MOD_RES 66 66 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 66 66 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 104 104 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 104 104 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 122 122 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 122 122 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 132 132 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 132 132 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 143 143 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 143 143 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 159 159 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 166 166 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 273 273 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 277 277 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6R2}.
MOD_RES 334 334 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 334 334 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 346 346 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 410 410 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 410 410 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 417 417 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09622}.
MOD_RES 420 420 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 430 430 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 505 505 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 505 505 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
DISULFID 80 85 Redox-active. {ECO:0000250}.
CONFLICT 54 54 Y -> C (in Ref. 1; AAC53170).
{ECO:0000305}.
CONFLICT 144 144 Q -> T (in Ref. 2; BAE22867).
{ECO:0000305}.
CONFLICT 149 149 H -> L (in Ref. 2; BAE31961).
{ECO:0000305}.
CONFLICT 283 283 K -> E (in Ref. 2; BAE40693).
{ECO:0000305}.
SEQUENCE 509 AA; 54272 MW; 2C381852BAAD0441 CRC64;
MQSWSRVYRS LAKKGHFNRI SHGLQGVSSV PLRTYADQPI EADVTVIGSG PGGYVAAIKS
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEIPEVRLNL
EKMMEQKHSA VKALTGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS TQVIDTKNIL
VATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT
AVEFLGHVGG IGIDMEISKN FQRILQRQGF KFKLNTKVTG ATKKSDGKID VSVEAASGGK
AEVITCDVLL VCIGRRPFTQ NLGLEELGIE LDPKGRIPVN NRFQTKIPNI YAIGDVVAGP
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEFKIGK
FPFAANSRAK TNADTDGMVK ILGHKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI
ARVCHAHPTL SEAFREANLA AAFGKPINF


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Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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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

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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
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IBAN lautet DE8839050000107569353
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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
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San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
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София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
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GENTAUR Poland Sp. z o.o.


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TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

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GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
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Fax 02 36 00 65 94
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