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 KGD_MYCS2               Reviewed;        1227 AA.
A0R2B1; I7GDF5;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 1.
07-JUN-2017, entry version 84.
RecName: Full=Multifunctional 2-oxoglutarate metabolism enzyme;
AltName: Full=2-hydroxy-3-oxoadipate synthase;
Short=HOA synthase;
Short=HOAS;
EC=2.2.1.5;
AltName: Full=2-oxoglutarate carboxy-lyase;
AltName: Full=2-oxoglutarate decarboxylase;
AltName: Full=Alpha-ketoglutarate decarboxylase;
Short=KG decarboxylase;
Short=KGD;
EC=4.1.1.71;
AltName: Full=Alpha-ketoglutarate-glyoxylate carboligase;
Includes:
RecName: Full=2-oxoglutarate dehydrogenase E1 component;
Short=ODH E1 component;
EC=1.2.4.2;
AltName: Full=Alpha-ketoglutarate dehydrogenase E1 component;
Short=KDH E1 component;
Includes:
RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
EC=2.3.1.61;
AltName: Full=2-oxoglutarate dehydrogenase complex E2 component;
Short=ODH E2 component;
Short=OGDC-E2;
AltName: Full=Dihydrolipoamide succinyltransferase;
Name=kgd; Synonyms=sucA; OrderedLocusNames=MSMEG_5049, MSMEI_4922;
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=246196;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700084 / mc(2)155;
Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
Fraser C.M.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700084 / mc(2)155;
PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
"Interrupted coding sequences in Mycobacterium smegmatis: authentic
mutations or sequencing errors?";
Genome Biol. 8:R20.1-R20.9(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 700084 / mc(2)155;
PubMed=18955433; DOI=10.1101/gr.081901.108;
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
"Ortho-proteogenomics: multiple proteomes investigation through
orthology and a new MS-based protocol.";
Genome Res. 19:128-135(2009).
[4]
FUNCTION IN 2-OXOGLUTARATE DECARBOXYLATION, ENZYME REGULATION, KINETIC
PARAMETERS, AND INTERACTION WITH GARA.
STRAIN=ATCC 700084 / mc(2)155;
PubMed=19019160; DOI=10.1111/j.1365-2958.2008.06489.x;
O'Hare H.M., Duran R., Cervenansky C., Bellinzoni M., Wehenkel A.M.,
Pritsch O., Obal G., Baumgartner J., Vialaret J., Johnsson K.,
Alzari P.M.;
"Regulation of glutamate metabolism by protein kinases in
mycobacteria.";
Mol. Microbiol. 70:1408-1423(2008).
[5]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 116-1227 IN COMPLEXES WITH
THIAMINE PYROPHOSPHATE; ACETYL-COA; ENAMINE-THDP REACTION INTERMEDIATE
AND MAGNESIUM, FUNCTION AS A MULTIFUNCTIONAL ENZYME, CATALYTIC
ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT, PATHWAY, MUTAGENESIS
OF HIS-539; HIS-579; HIS-747; ARG-781; HIS-1020; GLU-1034 AND
ARG-1062, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 700084 / mc(2)155;
PubMed=21867916; DOI=10.1016/j.chembiol.2011.06.004;
Wagner T., Bellinzoni M., Wehenkel A., O'Hare H.M., Alzari P.M.;
"Functional plasticity and allosteric regulation of alpha-
ketoglutarate decarboxylase in central mycobacterial metabolism.";
Chem. Biol. 18:1011-1020(2011).
-!- FUNCTION: Shows three enzymatic activities that share a first
common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-
ketoglutarate, KG), leading to the formation of an enamine-
thiamine-PP intermediate upon decarboxylation. Thus, displays KGD
activity, catalyzing the decarboxylation from five-carbon 2-
oxoglutarate to four-carbon succinate semialdehyde (SSA). Also
catalyzes C-C bond formation between the activated aldehyde formed
after decarboxylation of alpha-ketoglutarate and the carbonyl of
glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which
spontaneously decarboxylates to form 5-hydroxylevulinate (HLA).
And is also a component of the 2-oxoglutarate dehydrogenase (ODH)
complex, that catalyzes the overall conversion of 2-oxoglutarate
to succinyl-CoA and CO(2). The KG decarboxylase and KG
dehydrogenase reactions provide two alternative, tightly
regulated, pathways connecting the oxidative and reductive
branches of the TCA cycle. {ECO:0000269|PubMed:19019160,
ECO:0000269|PubMed:21867916}.
-!- CATALYTIC ACTIVITY: 2-oxoglutarate + glyoxylate = 2-hydroxy-3-
oxoadipate + CO(2). {ECO:0000269|PubMed:21867916}.
-!- CATALYTIC ACTIVITY: 2-oxoglutarate = succinate semialdehyde +
CO(2). {ECO:0000269|PubMed:21867916}.
-!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
{ECO:0000269|PubMed:21867916}.
-!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)-
(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-
succinyldihydrolipoyl)lysine. {ECO:0000269|PubMed:21867916}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:21867916};
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Evidence={ECO:0000269|PubMed:21867916};
-!- ENZYME REGULATION: Alpha-ketoglutarate dehydrogenase and
decarboxylase activities are inhibited by unphosphorylated GarA,
and allosterically activated by acetyl-CoA, the main substrate of
the TCA cycle. Both the phosphoadenosine and acetyl moieties of
acetyl-CoA are important for activation because neither CoA nor
the synthetic compound S-(2-acetamidoethyl)-ethanethioate (which
mimics the terminal acetyl-phosphopantetheine group of acetyl-CoA)
has an activation effect. {ECO:0000269|PubMed:19019160,
ECO:0000269|PubMed:21867916}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.54 mM for alpha-ketoglutarate
{ECO:0000269|PubMed:19019160};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
succinate from 2-oxoglutarate (transferase route): step 1/2.
{ECO:0000269|PubMed:21867916}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
{ECO:0000269|PubMed:21867916}.
-!- SUBUNIT: Homodimer. Interacts with the FHA domain of
unphosphorylated GarA. The 2-oxoglutarate dehydrogenase (ODH)
complex contains multiple copies of three enzymatic components: 2-
oxoglutarate dehydrogenase (E1), dihydrolipoamide
succinyltransferase (E2) and lipoamide dehydrogenase (E3).
{ECO:0000269|PubMed:19019160, ECO:0000269|PubMed:21867916}.
-!- DOMAIN: Is a fusion protein with two major domains exhibiting
structural features of an E1 and E2 protein, and a short sequence
stretch of E1 localized at the N-terminus, which is connected by a
linker region to the rest of the protein. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show any ODH
activity, in contrast to wild-type, demonstrating that this
protein is part of a functional ODH complex in mycobacteria.
{ECO:0000269|PubMed:21867916}.
-!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. Kgd
subfamily. {ECO:0000305}.
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EMBL; CP000480; ABK74238.1; -; Genomic_DNA.
EMBL; CP001663; AFP41366.1; -; Genomic_DNA.
RefSeq; WP_011730279.1; NZ_CP009494.1.
RefSeq; YP_889299.1; NC_008596.1.
PDB; 2XT6; X-ray; 2.74 A; A/B=116-1227.
PDB; 2XT9; X-ray; 2.20 A; A=361-1227.
PDB; 2XTA; X-ray; 2.20 A; A/B/C/D=361-1227.
PDB; 2Y0P; X-ray; 2.40 A; A/B/C/D=361-1227.
PDB; 2YIC; X-ray; 1.96 A; A/B/C/D=361-1227.
PDB; 2YID; X-ray; 2.25 A; A/B/C/D=361-1227.
PDB; 3ZHQ; X-ray; 2.50 A; A/B/C/D=361-1227.
PDB; 3ZHR; X-ray; 2.10 A; A/B/C/D=361-1227.
PDB; 3ZHS; X-ray; 2.10 A; A/B/C/D=361-1227.
PDB; 3ZHT; X-ray; 2.15 A; A/B/C/D=361-1227.
PDB; 3ZHU; X-ray; 2.30 A; A/B/C/D=361-1227.
PDB; 3ZHV; X-ray; 2.30 A; A/B/C/D=361-1227.
PDBsum; 2XT6; -.
PDBsum; 2XT9; -.
PDBsum; 2XTA; -.
PDBsum; 2Y0P; -.
PDBsum; 2YIC; -.
PDBsum; 2YID; -.
PDBsum; 3ZHQ; -.
PDBsum; 3ZHR; -.
PDBsum; 3ZHS; -.
PDBsum; 3ZHT; -.
PDBsum; 3ZHU; -.
PDBsum; 3ZHV; -.
ProteinModelPortal; A0R2B1; -.
SMR; A0R2B1; -.
IntAct; A0R2B1; 1.
STRING; 246196.MSMEG_5049; -.
PRIDE; A0R2B1; -.
EnsemblBacteria; ABK74238; ABK74238; MSMEG_5049.
EnsemblBacteria; AFP41366; AFP41366; MSMEI_4922.
GeneID; 4535402; -.
KEGG; msb:LJ00_24970; -.
KEGG; msg:MSMEI_4922; -.
KEGG; msm:MSMEG_5049; -.
PATRIC; fig|246196.19.peg.4927; -.
eggNOG; ENOG4105C7P; Bacteria.
eggNOG; COG0508; LUCA.
eggNOG; COG0567; LUCA.
HOGENOM; HOG000259587; -.
KO; K01616; -.
OMA; IDMVCYR; -.
OrthoDB; POG091H03SK; -.
BRENDA; 4.1.1.71; 3512.
UniPathway; UPA00223; UER00997.
UniPathway; UPA00223; UER01001.
EvolutionaryTrace; A0R2B1; -.
Proteomes; UP000000757; Chromosome.
Proteomes; UP000006158; Chromosome.
GO; GO:0050439; F:2-hydroxy-3-oxoadipate synthase activity; IEA:UniProtKB-EC.
GO; GO:0008683; F:2-oxoglutarate decarboxylase activity; IEA:UniProtKB-EC.
GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
InterPro; IPR032106; 2-oxogl_dehyd_N.
InterPro; IPR011603; 2oxoglutarate_DH_E1.
InterPro; IPR001017; DH_E1.
InterPro; IPR031717; KGD_C.
InterPro; IPR029061; THDP-binding.
InterPro; IPR005475; Transketolase-like_Pyr-bd.
PANTHER; PTHR23152; PTHR23152; 1.
Pfam; PF00198; 2-oxoacid_dh; 1.
Pfam; PF16078; 2-oxogl_dehyd_N; 1.
Pfam; PF00676; E1_dh; 1.
Pfam; PF16870; OxoGdeHyase_C; 1.
Pfam; PF02779; Transket_pyr; 1.
PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
SMART; SM00861; Transket_pyr; 1.
SUPFAM; SSF52518; SSF52518; 2.
TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Allosteric enzyme; Coiled coil;
Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding;
Multifunctional enzyme; Oxidoreductase; Reference proteome;
Thiamine pyrophosphate; Transferase; Tricarboxylic acid cycle.
CHAIN 1 1227 Multifunctional 2-oxoglutarate metabolism
enzyme.
/FTId=PRO_0000310718.
REGION 1 41 2-oxoglutarate dehydrogenase E1, N-
terminal part.
REGION 42 88 Linker.
REGION 89 335 Succinyltransferase E2.
REGION 336 1227 2-oxoglutarate dehydrogenase E1, C-
terminal part.
REGION 539 540 Thiamine pyrophosphate binding.
REGION 604 606 Thiamine pyrophosphate binding.
REGION 645 647 Thiamine pyrophosphate binding.
REGION 1089 1092 Allosteric activator.
REGION 1149 1150 Allosteric activator.
COILED 783 814 {ECO:0000255}.
ACT_SITE 314 314 Proton acceptor; for succinyltransferase
activity. {ECO:0000250}.
METAL 645 645 Magnesium.
METAL 678 678 Magnesium.
METAL 680 680 Magnesium; via carbonyl oxygen.
BINDING 579 579 2-oxoglutarate.
BINDING 604 604 2-oxoglutarate.
BINDING 952 952 Thiamine pyrophosphate.
BINDING 1020 1020 2-oxoglutarate.
BINDING 1038 1038 Allosteric activator.
BINDING 1054 1054 Allosteric activator.
BINDING 1142 1142 Allosteric activator.
MUTAGEN 539 539 H->A: Loss of KG decarboxylase activity.
{ECO:0000269|PubMed:21867916}.
MUTAGEN 579 579 H->A: Loss of KG decarboxylase activity.
{ECO:0000269|PubMed:21867916}.
MUTAGEN 747 747 H->A: 40-fold decrease in KG
decarboxylase activity.
{ECO:0000269|PubMed:21867916}.
MUTAGEN 781 781 R->A: Increase in KG decarboxylase
activity. {ECO:0000269|PubMed:21867916}.
MUTAGEN 1020 1020 H->A: Loss of KG decarboxylase activity.
{ECO:0000269|PubMed:21867916}.
MUTAGEN 1034 1034 E->A: Loss of activation by acetyl-CoA.
{ECO:0000269|PubMed:21867916}.
MUTAGEN 1062 1062 R->A: Loss of activation by acetyl-CoA.
{ECO:0000269|PubMed:21867916}.
STRAND 124 132 {ECO:0000244|PDB:2XT6}.
HELIX 134 149 {ECO:0000244|PDB:2XT6}.
HELIX 157 171 {ECO:0000244|PDB:2XT6}.
HELIX 173 176 {ECO:0000244|PDB:2XT6}.
STRAND 178 189 {ECO:0000244|PDB:2XT6}.
STRAND 196 199 {ECO:0000244|PDB:2XT6}.
STRAND 213 216 {ECO:0000244|PDB:2XT6}.
HELIX 219 221 {ECO:0000244|PDB:2XT6}.
HELIX 224 238 {ECO:0000244|PDB:2XT6}.
TURN 239 241 {ECO:0000244|PDB:2XT6}.
HELIX 245 247 {ECO:0000244|PDB:2XT6}.
STRAND 252 256 {ECO:0000244|PDB:2XT6}.
STRAND 275 280 {ECO:0000244|PDB:2XT6}.
HELIX 294 300 {ECO:0000244|PDB:2XT6}.
STRAND 305 313 {ECO:0000244|PDB:2XT6}.
TURN 314 316 {ECO:0000244|PDB:2XT6}.
HELIX 319 332 {ECO:0000244|PDB:2XT6}.
HELIX 336 345 {ECO:0000244|PDB:2XT6}.
HELIX 367 380 {ECO:0000244|PDB:2YIC}.
HELIX 381 383 {ECO:0000244|PDB:2YIC}.
HELIX 395 398 {ECO:0000244|PDB:2YIC}.
TURN 401 403 {ECO:0000244|PDB:2XT6}.
HELIX 406 408 {ECO:0000244|PDB:2XTA}.
HELIX 412 414 {ECO:0000244|PDB:2XT9}.
STRAND 416 419 {ECO:0000244|PDB:2YIC}.
STRAND 429 431 {ECO:0000244|PDB:2XT9}.
HELIX 432 443 {ECO:0000244|PDB:2YIC}.
STRAND 444 450 {ECO:0000244|PDB:2YIC}.
HELIX 457 467 {ECO:0000244|PDB:2YIC}.
HELIX 476 499 {ECO:0000244|PDB:2YIC}.
STRAND 500 502 {ECO:0000244|PDB:3ZHS}.
HELIX 504 506 {ECO:0000244|PDB:2YIC}.
HELIX 514 527 {ECO:0000244|PDB:2YIC}.
STRAND 531 536 {ECO:0000244|PDB:2YIC}.
HELIX 542 548 {ECO:0000244|PDB:2YIC}.
HELIX 554 557 {ECO:0000244|PDB:2YIC}.
TURN 558 560 {ECO:0000244|PDB:2YIC}.
HELIX 567 570 {ECO:0000244|PDB:2YID}.
STRAND 571 573 {ECO:0000244|PDB:2YID}.
HELIX 576 578 {ECO:0000244|PDB:2YIC}.
STRAND 582 587 {ECO:0000244|PDB:2YIC}.
STRAND 589 592 {ECO:0000244|PDB:2YIC}.
STRAND 594 599 {ECO:0000244|PDB:2YIC}.
TURN 606 609 {ECO:0000244|PDB:2YIC}.
HELIX 610 624 {ECO:0000244|PDB:2YIC}.
STRAND 630 632 {ECO:0000244|PDB:2YIC}.
STRAND 637 644 {ECO:0000244|PDB:2YIC}.
HELIX 645 650 {ECO:0000244|PDB:2YIC}.
HELIX 652 658 {ECO:0000244|PDB:2YIC}.
TURN 659 662 {ECO:0000244|PDB:2YIC}.
TURN 664 666 {ECO:0000244|PDB:2YIC}.
STRAND 672 677 {ECO:0000244|PDB:2YIC}.
HELIX 686 689 {ECO:0000244|PDB:2YIC}.
STRAND 691 694 {ECO:0000244|PDB:2YIC}.
HELIX 697 702 {ECO:0000244|PDB:2YIC}.
STRAND 706 710 {ECO:0000244|PDB:2YIC}.
HELIX 714 731 {ECO:0000244|PDB:2YIC}.
STRAND 735 740 {ECO:0000244|PDB:2YIC}.
HELIX 753 755 {ECO:0000244|PDB:2YIC}.
HELIX 758 764 {ECO:0000244|PDB:2YIC}.
HELIX 770 780 {ECO:0000244|PDB:2YIC}.
HELIX 786 812 {ECO:0000244|PDB:2YIC}.
HELIX 822 824 {ECO:0000244|PDB:2YID}.
HELIX 837 846 {ECO:0000244|PDB:2YIC}.
TURN 858 860 {ECO:0000244|PDB:2YIC}.
HELIX 861 873 {ECO:0000244|PDB:2YIC}.
HELIX 878 891 {ECO:0000244|PDB:2YIC}.
STRAND 895 900 {ECO:0000244|PDB:2YIC}.
TURN 901 905 {ECO:0000244|PDB:2YIC}.
STRAND 913 916 {ECO:0000244|PDB:2YIC}.
TURN 918 920 {ECO:0000244|PDB:2YIC}.
HELIX 926 931 {ECO:0000244|PDB:2YIC}.
STRAND 942 947 {ECO:0000244|PDB:2YIC}.
HELIX 953 965 {ECO:0000244|PDB:2YIC}.
STRAND 969 974 {ECO:0000244|PDB:2YIC}.
HELIX 978 984 {ECO:0000244|PDB:2YIC}.
HELIX 985 990 {ECO:0000244|PDB:2YIC}.
TURN 991 994 {ECO:0000244|PDB:2YIC}.
HELIX 995 999 {ECO:0000244|PDB:2YIC}.
STRAND 1006 1010 {ECO:0000244|PDB:2YIC}.
STRAND 1014 1016 {ECO:0000244|PDB:2YIC}.
HELIX 1025 1031 {ECO:0000244|PDB:2YIC}.
STRAND 1034 1036 {ECO:0000244|PDB:3ZHT}.
STRAND 1038 1040 {ECO:0000244|PDB:2YIC}.
HELIX 1045 1057 {ECO:0000244|PDB:2YIC}.
STRAND 1064 1068 {ECO:0000244|PDB:2YIC}.
HELIX 1071 1074 {ECO:0000244|PDB:2YIC}.
STRAND 1076 1078 {ECO:0000244|PDB:2Y0P}.
HELIX 1082 1086 {ECO:0000244|PDB:2YIC}.
STRAND 1092 1094 {ECO:0000244|PDB:2YIC}.
HELIX 1097 1100 {ECO:0000244|PDB:2YIC}.
HELIX 1106 1108 {ECO:0000244|PDB:2YIC}.
STRAND 1111 1115 {ECO:0000244|PDB:2YIC}.
HELIX 1119 1130 {ECO:0000244|PDB:2YIC}.
STRAND 1135 1140 {ECO:0000244|PDB:2YIC}.
STRAND 1142 1145 {ECO:0000244|PDB:2YIC}.
HELIX 1148 1156 {ECO:0000244|PDB:2YIC}.
STRAND 1163 1171 {ECO:0000244|PDB:2YIC}.
STRAND 1174 1176 {ECO:0000244|PDB:2YID}.
HELIX 1177 1187 {ECO:0000244|PDB:2YIC}.
HELIX 1189 1192 {ECO:0000244|PDB:2YIC}.
STRAND 1196 1200 {ECO:0000244|PDB:2YIC}.
STRAND 1204 1207 {ECO:0000244|PDB:2YIC}.
HELIX 1211 1225 {ECO:0000244|PDB:2YIC}.
SEQUENCE 1227 AA; 135944 MW; 76C5BFFD1638A391 CRC64;
MSSSPSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTTDSAS NGRTTTAAPV
TPPTPAPAPA PEPKAAPKPA AKTEAKPAKP AKSATPAKGD ESQILRGAAA AVVKNMNASL
EVPTATSVRA IPAKLMIDNR VVINNHLKRT RGGKISFTHL LGYAIVQAVK KFPNMNRHFA
VVDGKPTAIT PAHTNLGLAI DLQGKDGNRS LVVAAIKRCE TMRFGQFIAA YEDIVRRARD
GKLTAEDFSG VTISLTNPGT LGTVHSVPRL MQGQGAIIGA GAMEYPAEFQ GASEERIADL
GIGKLITLTS TYDHRIIQGA ESGDFLRTIH QLLLDDDFFD EIFRELGIPY EPVRWRTDNP
DSIEDKNARV IELIAAYRNR GHLMADIDPL RLDNTRFRSH PDLDVNSHGL TLWDLDREFK
VDGFAGVQRK KLRDILSVLR DAYCRHVGVE YTHILEPEQQ RWIQERVETK HDKPTVAEQK
YILSKLNAAE AFETFLQTKY VGQKRFSLEG AETVIPMMDA VIDQCAEHGL DEVVIAMPHR
GRLNVLANIV GKPYSQIFSE FEGNLNPSQA HGSGDVKYHL GATGTYIQMF GDNDIEVSLT
ANPSHLEAVD PVLEGLVRAK QDLLDTGEEG SDNRFSVVPL MLHGDAAFAG QGVVAETLNL
ALLRGYRTGG TIHIVVNNQI GFTTAPTDSR SSEYCTDVAK MIGAPIFHVN GDDPEACAWV
ARLAVDFRQA FKKDVVIDML CYRRRGHNEG DDPSMTQPYM YDVIDTKRGS RKAYTEALIG
RGDISMKEAE DALRDYQGQL ERVFNEVREL EKHEIEPSES VEADQQIPSK LATAVDKAML
QRIGDAHLAL PEGFTVHPRV RPVLEKRREM AYEGRIDWAF AELLALGSLI AEGKLVRLSG
QDTQRGTFTQ RHAVIVDRKT GEEFTPLQLL ATNPDGTPTG GKFLVYNSAL SEFAAVGFEY
GYSVGNPDAM VLWEAQFGDF VNGAQSIIDE FISSGEAKWG QLSDVVLLLP HGHEGQGPDH
TSGRIERFLQ LWAEGSMTIA MPSTPANYFH LLRRHGKDGI QRPLIVFTPK SMLRNKAAVS
DIRDFTESKF RSVLEEPMYT DGEGDRNKVT RLLLTSGKIY YELAARKAKE NREDVAIVRI
EQLAPLPRRR LAETLDRYPN VKEKFWVQEE PANQGAWPSF GLTLPEILPD HFTGLKRISR
RAMSAPSSGS SKVHAVEQQE ILDTAFG


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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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