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Dual specificity phosphatase Cdc25 (EC 3.1.3.48) (Arath;CDC25) (Arsenate reductase) (AtASR) (Arsenate reductase 2) (EC 1.20.4.1) (Sulfurtransferase 5) (AtStr5)

 CDC25_ARATH             Reviewed;         146 AA.
 Q8GY31; Q8LC90; Q9LZE1;
 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2003, sequence version 1.
 25-OCT-2017, entry version 111.
 RecName: Full=Dual specificity phosphatase Cdc25 {ECO:0000303|PubMed:15329414};
          EC=3.1.3.48 {ECO:0000269|PubMed:15329414};
 AltName: Full=Arath;CDC25 {ECO:0000303|PubMed:15329414};
 AltName: Full=Arsenate reductase {ECO:0000303|PubMed:16507083};
          Short=AtASR {ECO:0000303|PubMed:16507083};
 AltName: Full=Arsenate reductase 2 {ECO:0000303|PubMed:16567632};
          EC=1.20.4.1 {ECO:0000269|PubMed:16766666};
 AltName: Full=Sulfurtransferase 5 {ECO:0000303|PubMed:17408957};
          Short=AtStr5 {ECO:0000303|PubMed:17408957};
 Name=CDC25 {ECO:0000303|PubMed:15329414};
 Synonyms=ACR2 {ECO:0000303|PubMed:16567632},
 ASR {ECO:0000303|PubMed:16507083}, STR5 {ECO:0000303|PubMed:17408957};
 OrderedLocusNames=At5g03455 {ECO:0000312|Araport:AT5G03455};
 ORFNames=F12E4_220 {ECO:0000312|EMBL:CAB83305.1};
 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 [LARGE SCALE GENOMIC DNA].
 STRAIN=cv. Columbia;
 PubMed=11130714; DOI=10.1038/35048507;
 Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
 Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
 Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
 Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
 Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
 Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
 Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
 Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
 Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
 Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
 Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
 Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
 Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
 Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
 Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
 Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
 Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
 Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
 Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
 van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
 Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
 Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
 Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
 Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
 "Sequence and analysis of chromosome 5 of the plant Arabidopsis
 thaliana.";
 Nature 408:823-826(2000).
 [2]
 GENOME REANNOTATION.
 STRAIN=cv. Columbia;
 The Arabidopsis Information Portal (Araport);
 Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=cv. Columbia;
 PubMed=11910074; DOI=10.1126/science.1071006;
 Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
 Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
 Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
 Shibata K., Shinagawa A., Shinozaki K.;
 "Functional annotation of a full-length Arabidopsis cDNA collection.";
 Science 296:141-145(2002).
 [4]
 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).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
 Feldmann K.A.;
 "Full-length cDNA from Arabidopsis thaliana.";
 Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
 [6]
 TISSUE SPECIFICITY.
 PubMed=15720653; DOI=10.1111/j.1469-8137.2004.01288.x;
 Sorrell D.A., Chrimes D., Dickinson J.R., Rogers H.J., Francis D.;
 "The Arabidopsis CDC25 induces a short cell length when overexpressed
 in fission yeast: evidence for cell cycle function.";
 New Phytol. 165:425-428(2005).
 [7]
 FUNCTION, AND DISRUPTION PHENOTYPE.
 PubMed=16507083; DOI=10.1111/j.1365-313X.2005.02651.x;
 Bleeker P.M., Hakvoort H.W., Bliek M., Souer E., Schat H.;
 "Enhanced arsenate reduction by a CDC25-like tyrosine phosphatase
 explains increased phytochelatin accumulation in arsenate-tolerant
 Holcus lanatus.";
 Plant J. 45:917-929(2006).
 [8]
 FUNCTION, AND CATALYTIC ACTIVITY.
 PubMed=16766666; DOI=10.1104/pp.106.084079;
 Ellis D.R., Gumaelius L., Indriolo E., Pickering I.J., Banks J.A.,
 Salt D.E.;
 "A novel arsenate reductase from the arsenic hyperaccumulating fern
 Pteris vittata.";
 Plant Physiol. 141:1544-1554(2006).
 [9]
 FUNCTION, AND TISSUE SPECIFICITY.
 PubMed=16567632; DOI=10.1073/pnas.0509770102;
 Dhankher O.P., Rosen B.P., McKinney E.C., Meagher R.B.;
 "Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced
 for arsenate reductase (ACR2).";
 Proc. Natl. Acad. Sci. U.S.A. 103:5413-5418(2006).
 [10]
 GENE FAMILY.
 PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
 Bartels A., Mock H.P., Papenbrock J.;
 "Differential expression of Arabidopsis sulfurtransferases under
 various growth conditions.";
 Plant Physiol. Biochem. 45:178-187(2007).
 [11]
 DISRUPTION PHENOTYPE.
 PubMed=20647223; DOI=10.1093/aob/mcq142;
 Spadafora N.D., Doonan J.H., Herbert R.J., Bitonti M.B., Wallace E.,
 Rogers H.J., Francis D.;
 "Arabidopsis T-DNA insertional lines for CDC25 are hypersensitive to
 hydroxyurea but not to zeocin or salt stress.";
 Ann. Bot. 107:1183-1192(2011).
 [12]
 3D-STRUCTURE MODELING, AND FUNCTION.
 PubMed=22562211; DOI=10.1007/s00894-012-1419-y;
 Nahar N., Rahman A., Mos M., Warzecha T., Algerin M., Ghosh S.,
 Johnson-Brousseau S., Mandal A.;
 "In silico and in vivo studies of an Arabidopsis thaliana gene, ACR2,
 putatively involved in arsenic accumulation in plants.";
 J. Mol. Model. 18:4249-4262(2012).
 [13]
 FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
 PubMed=22879969; DOI=10.1371/journal.pone.0042408;
 Liu W., Schat H., Bliek M., Chen Y., McGrath S.P., George G.,
 Salt D.E., Zhao F.J.;
 "Knocking out ACR2 does not affect arsenic redox status in Arabidopsis
 thaliana: implications for as detoxification and accumulation in
 plants.";
 PLoS ONE 7:E42408-E42408(2012).
 [14]
 DISRUPTION PHENOTYPE.
 PubMed=25099865; DOI=10.1038/ncomms5617;
 Sanchez-Bermejo E., Castrillo G., del Llano B., Navarro C.,
 Zarco-Fernandez S., Martinez-Herrera D.J., Leo-del Puerto Y.,
 Munoz R., Camara C., Paz-Ares J., Alonso-Blanco C., Leyva A.;
 "Natural variation in arsenate tolerance identifies an arsenate
 reductase in Arabidopsis thaliana.";
 Nat. Commun. 5:4617-4617(2014).
 [15]
 FUNCTION, AND DISRUPTION PHENOTYPE.
 PubMed=25464340; DOI=10.1371/journal.pbio.1002009;
 Chao D.Y., Chen Y., Chen J., Shi S., Chen Z., Wang C., Danku J.M.,
 Zhao F.J., Salt D.E.;
 "Genome-wide association mapping identifies a new arsenate reductase
 enzyme critical for limiting arsenic accumulation in plants.";
 PLoS Biol. 12:E1002009-E1002009(2014).
 [16]
 STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC,
 BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-145.
 PubMed=15336525; DOI=10.1016/j.bbrc.2004.07.182;
 Landrieu I., Hassan S., Sauty M., Dewitte F., Wieruszeski J.-M.,
 Inze D., de Veylder L., Lippens G.;
 "Characterization of the Arabidopsis thaliana Arath;CDC25 dual-
 specificity tyrosine phosphatase.";
 Biochem. Biophys. Res. Commun. 322:734-739(2004).
 [17]
 STRUCTURE BY NMR OF 15-146 OF CYS-86 MUTANT IN COMPLEX WITH ZINC,
 FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
 PROPERTIES, AND MUTAGENESIS OF CYS-86.
 PubMed=15329414; DOI=10.1073/pnas.0405248101;
 Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K.,
 Hassan S., Wieruszeski J.-M., Corellou F., Faure J.-D.,
 Van Montagu M., Inze D., Lippens G.;
 "A small CDC25 dual-specificity tyrosine-phosphatase isoform in
 Arabidopsis thaliana.";
 Proc. Natl. Acad. Sci. U.S.A. 101:13380-13385(2004).
 [18]
 ERRATUM.
 DOI=10.1073/pnas.0407263101;
 Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K.,
 Hassan S., Wieruszeski J.M., Corellou F., Faure J.D., Van Montagu M.,
 Inze D., Lippens G.;
 Proc. Natl. Acad. Sci. U.S.A. 101:16391-16391(2004).
 -!- FUNCTION: Tyrosine protein phosphatase that dephosphorylates CDK
     complex and activate its kinase activity in vitro.
     {ECO:0000269|PubMed:15329414, ECO:0000269|PubMed:16766666}.
 -!- FUNCTION: Arsenate reductase that plays a major role in the
     reduction of arsenate to arsenite and arsenic retention in roots
     (PubMed:16567632). Has an in vitro and in vivo arsenate reductase
     activity (PubMed:16507083, PubMed:16766666, PubMed:22562211).
     Plays no role in arsenic metabolism (PubMed:22879969,
     PubMed:25464340). {ECO:0000269|PubMed:16507083,
     ECO:0000269|PubMed:16567632, ECO:0000269|PubMed:16766666,
     ECO:0000269|PubMed:22879969, ECO:0000269|PubMed:25464340}.
 -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
     tyrosine + phosphate. {ECO:0000269|PubMed:15329414}.
 -!- CATALYTIC ACTIVITY: Arsenate + glutaredoxin = arsenite +
     glutaredoxin disulfide + H(2)O. {ECO:0000269|PubMed:16766666}.
 -!- ENZYME REGULATION: Inhibited by NSC95397.
     {ECO:0000269|PubMed:15329414}.
 -!- BIOPHYSICOCHEMICAL PROPERTIES:
     Kinetic parameters:
       KM=50 mM for para-nitrophenyl phosphate
       {ECO:0000269|PubMed:15329414, ECO:0000269|PubMed:15336525};
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
 -!- TISSUE SPECIFICITY: Expressed in roots and at lower levels in
     shoots (at protein level). Expressed in leaves, stems and flowers.
     {ECO:0000269|PubMed:15720653, ECO:0000269|PubMed:16567632,
     ECO:0000269|PubMed:22879969}.
 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
     conditions, but plants show reduced root size when grown in
     presence of hydroxyurea (PubMed:20647223). No visible phenotype,
     but decreased accumulation of total arsenic in shoots
     (PubMed:16507083). No effect on arsenate sensitivity
     (PubMed:25099865). No effect on the accumulation of arsenate in
     roots, efflux of arsenite or uptake of arsenate, or the total
     arsenic accumulation in shoots (PubMed:22879969, PubMed:25464340).
     {ECO:0000269|PubMed:16507083, ECO:0000269|PubMed:20647223,
     ECO:0000269|PubMed:22879969, ECO:0000269|PubMed:25099865,
     ECO:0000269|PubMed:25464340}.
 -!- MISCELLANEOUS: Binds 1 zinc ion which is not required for enzyme
     activity (PubMed:15329414). Plants silencing ACR2 show increased
     sensitivity to arsenate but not arsenite (PubMed:16567632).
     {ECO:0000305|PubMed:15329414, ECO:0000305|PubMed:16567632}.
 -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAM63780.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
     Sequence=CAB83305.1; 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; AL162751; CAB83305.1; ALT_SEQ; Genomic_DNA.
 EMBL; CP002688; AED90607.1; -; Genomic_DNA.
 EMBL; AK117898; BAC42537.1; -; mRNA.
 EMBL; BT003658; AAO39886.1; -; mRNA.
 EMBL; AY086729; AAM63780.1; ALT_INIT; mRNA.
 PIR; T48370; T48370.
 RefSeq; NP_568119.1; NM_120425.3.
 UniGene; At.43043; -.
 PDB; 1T3K; NMR; -; A=15-146.
 PDBsum; 1T3K; -.
 DisProt; DP00916; -.
 ProteinModelPortal; Q8GY31; -.
 SMR; Q8GY31; -.
 BioGrid; 17108; 3.
 IntAct; Q8GY31; 3.
 STRING; 3702.AT5G03455.1; -.
 PaxDb; Q8GY31; -.
 EnsemblPlants; AT5G03455.1; AT5G03455.1; AT5G03455.
 GeneID; 831832; -.
 Gramene; AT5G03455.1; AT5G03455.1; AT5G03455.
 KEGG; ath:AT5G03455; -.
 Araport; AT5G03455; -.
 TAIR; locus:505006579; AT5G03455.
 eggNOG; ENOG410IQGW; Eukaryota.
 eggNOG; ENOG4111VH0; LUCA.
 HOGENOM; HOG000162894; -.
 InParanoid; Q8GY31; -.
 KO; K18065; -.
 OMA; DYIGGHI; -.
 OrthoDB; EOG09360QPX; -.
 PhylomeDB; Q8GY31; -.
 BioCyc; ARA:AT5G03455-MONOMER; -.
 SABIO-RK; Q8GY31; -.
 EvolutionaryTrace; Q8GY31; -.
 PRO; PR:Q8GY31; -.
 Proteomes; UP000006548; Chromosome 5.
 ExpressionAtlas; Q8GY31; baseline and differential.
 Genevisible; Q8GY31; AT.
 GO; GO:0009507; C:chloroplast; IDA:TAIR.
 GO; GO:0005739; C:mitochondrion; IDA:TAIR.
 GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:TAIR.
 GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
 GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
 Gene3D; 3.40.250.10; -; 1.
 InterPro; IPR001763; Rhodanese-like_dom.
 InterPro; IPR036873; Rhodanese-like_dom_sf.
 Pfam; PF00581; Rhodanese; 1.
 SMART; SM00450; RHOD; 1.
 SUPFAM; SSF52821; SSF52821; 1.
 PROSITE; PS50206; RHODANESE_3; 1.
 1: Evidence at protein level;
 3D-structure; Cell cycle; Cell division; Complete proteome; Hydrolase;
 Metal-binding; Mitosis; Nucleus; Oxidoreductase; Protein phosphatase;
 Reference proteome; Zinc.
 CHAIN         1    146       Dual specificity phosphatase Cdc25.
                              /FTId=PRO_0000198663.
 DOMAIN       34    135       Rhodanese. {ECO:0000255|PROSITE-
                              ProRule:PRU00173}.
 REGION       45     48       Substrate-binding.
 REGION       68     71       Substrate-binding.
 REGION       90     92       Substrate-binding.
 COMPBIAS     11     14       Poly-Lys.
 ACT_SITE     86     86       Cysteine persulfide intermediate.
                              {ECO:0000255|PROSITE-ProRule:PRU00173}.
 METAL        53     53       Zinc. {ECO:0000269|PubMed:15329414,
                              ECO:0000269|PubMed:15336525}.
 METAL       134    134       Zinc. {ECO:0000269|PubMed:15329414,
                              ECO:0000269|PubMed:15336525}.
 METAL       136    136       Zinc. {ECO:0000269|PubMed:15329414,
                              ECO:0000269|PubMed:15336525}.
 METAL       141    141       Zinc. {ECO:0000269|PubMed:15329414,
                              ECO:0000269|PubMed:15336525}.
 MUTAGEN      86     86       C->S: Loss of phosphatase activity.
                              {ECO:0000269|PubMed:15329414}.
 MUTAGEN     145    145       C->S: No major structural changes.
                              {ECO:0000269|PubMed:15336525}.
 STRAND       19     24       {ECO:0000244|PDB:1T3K}.
 TURN         26     31       {ECO:0000244|PDB:1T3K}.
 STRAND       38     44       {ECO:0000244|PDB:1T3K}.
 HELIX        47     50       {ECO:0000244|PDB:1T3K}.
 STRAND       56     60       {ECO:0000244|PDB:1T3K}.
 STRAND       63     66       {ECO:0000244|PDB:1T3K}.
 HELIX        69     74       {ECO:0000244|PDB:1T3K}.
 STRAND       81     87       {ECO:0000244|PDB:1T3K}.
 STRAND       90     92       {ECO:0000244|PDB:1T3K}.
 HELIX        93    106       {ECO:0000244|PDB:1T3K}.
 STRAND      107    109       {ECO:0000244|PDB:1T3K}.
 STRAND      113    121       {ECO:0000244|PDB:1T3K}.
 HELIX       124    129       {ECO:0000244|PDB:1T3K}.
 SEQUENCE   146 AA;  16450 MW;  EA2DD0E79784D538 CRC64;
 MGRSIFSFFT KKKKMAMARS ISYITSTQLL PLHRRPNIAI IDVRDEERNY DGHIAGSLHY
 ASGSFDDKIS HLVQNVKDKD TLVFHCALSQ VRGPTCARRL VNYLDEKKED TGIKNIMILE
 RGFNGWEASG KPVCRCAEVP CKGDCA

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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