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

Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); Shikimate dehydrogenase (EC 1.1.1.25)]

 E3K2M0_PUCGT            Unreviewed;      1482 AA.
E3K2M0;
11-JAN-2011, integrated into UniProtKB/TrEMBL.
11-JAN-2011, sequence version 1.
22-NOV-2017, entry version 56.
RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_03143};
AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=DHQS {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=SK {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
ORFNames=PGTG_04545 {ECO:0000313|EMBL:EFP78589.1};
Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
(Black stem rust fungus).
Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP78589.1, ECO:0000313|Proteomes:UP000008783};
[1]
NUCLEOTIDE SEQUENCE.
STRAIN=CRL 75-36-700-3;
The Broad Institute Genome Sequencing Platform;
Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C.,
Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E.,
Brockman W., Young S., LaButti K., Sykes S., DeCaprio D., Crawford M.,
Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
Larson L., White J., Zeng Q., Kodira C., Yandava C., Alvarado L.,
O'Leary S., Szabo L., Dean R., Schein J.;
"The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL
75-36-700-3.";
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Proteomes:UP000008783}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CRL 75-36-700-3 / race SCCL
{ECO:0000313|Proteomes:UP000008783};
PubMed=21536894; DOI=10.1073/pnas.1019315108;
Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J.,
Cantarel B.L., Chiu R., Coutinho P.M., Feau N., Field M., Frey P.,
Gelhaye E., Goldberg J., Grabherr M.G., Kodira C.D., Kohler A.,
Kuees U., Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E.,
Murat C., Pangilinan J.L., Park R., Pearson M., Quesneville H.,
Rouhier N., Sakthikumar S., Salamov A.A., Schmutz J., Selles B.,
Shapiro H., Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y.,
Rouze P., Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
Grigoriev I.V., Szabo L.J., Martin F.;
"Obligate biotrophy features unraveled by the genomic analysis of rust
fungi.";
Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
-!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
reactions in prechorismate polyaromatic amino acid biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712173}.
-!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712185}.
-!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
= 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00726953}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00726958}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712174}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00712180}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00727023}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712175}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712177}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00726955}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712169}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712187}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00746849}.
-!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712186}.
-!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712182}.
-!- SIMILARITY: In the 4th section; belongs to the type-I 3-
dehydroquinase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712184}.
-!- SIMILARITY: In the C-terminal section; belongs to the shikimate
dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712181}.
-!- SIMILARITY: In the N-terminal section; belongs to the
dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514}.
-!- SIMILARITY: In the N-terminal section; belongs to the sugar
phosphate cyclases superfamily. Dehydroquinate synthase family.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00858969}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DS178270; EFP78589.1; -; Genomic_DNA.
RefSeq; XP_003323008.1; XM_003322960.2.
ProteinModelPortal; E3K2M0; -.
STRING; 5297.EFP78589; -.
EnsemblFungi; EFP78589; EFP78589; PGTG_04545.
GeneID; 10536354; -.
KEGG; pgr:PGTG_04545; -.
EuPathDB; FungiDB:PGTG_04545; -.
InParanoid; E3K2M0; -.
KO; K13830; -.
OMA; ITENARM; -.
OrthoDB; EOG092C0RWA; -.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000008783; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
CDD; cd00502; DHQase_I; 1.
CDD; cd01556; EPSP_synthase; 1.
CDD; cd00464; SK; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.65.10.10; -; 2.
HAMAP; MF_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR018508; 3-dehydroquinate_DH_AS.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR030960; DHQS/DOIS.
InterPro; IPR001381; DHquinase_I.
InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
InterPro; IPR006264; EPSP_synthase.
InterPro; IPR023193; EPSP_synthase_CS.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008289; Pentafunct_AroM.
InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
InterPro; IPR031322; Shikimate/glucono_kinase.
InterPro; IPR013708; Shikimate_DH-bd_N.
InterPro; IPR000623; Shikimate_kinase/TSH1.
InterPro; IPR023000; Shikimate_kinase_CS.
InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 1.
Pfam; PF01488; Shikimate_DH; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
Pfam; PF01202; SKI; 1.
PIRSF; PIRSF000514; Pentafunct_AroM; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR01356; aroA; 1.
TIGRFAMs; TIGR01093; aroD; 1.
PROSITE; PS01028; DEHYDROQUINASE_I; 1.
PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PROSITE; PS01128; SHIKIMATE_KINASE; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00759081};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00759081};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00726948};
Complete proteome {ECO:0000313|Proteomes:UP000008783};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00746907};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00726946};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00726960};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00727050};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00727049};
NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00726948};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172};
Reference proteome {ECO:0000313|Proteomes:UP000008783};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00726946};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00719910}.
DOMAIN 4 222 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 274 696 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1182 1265 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 1311 1358 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 34 37 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 736 743 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 248 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 128 132 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1177 1482 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 124 124 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 139 139 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 684 684 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1063 1063 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1091 1091 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 49 49 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 135 135 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 151 151 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 16 16 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 17 17 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 45 45 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 114 114 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 135 135 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 151 151 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 220 220 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1482 AA; 161128 MW; 5593BB4EBBD163DB CRC64;
MATFGSLTAI DTPLGKNLVG AFWQPSFIFI DASYLETLPE REFVNGMAEM IKTAAIWDES
QFEKLESNVD SIRSAVLSPP PRDPINPFPG RDLASRSQAQ KLLLEVIADS VGVKSEVVTK
DEKETGLRNL VNFGHTIGHA IEAVLTPAIL HGECVSIGMI LEAEVARARG CLSSSAIARL
SKCLKAHGLP VSLTDPRILS SPNAPNLNLD RLLDLMSVDK KNEGKVKKIV LLSRIGKTLE
ERATGVEDSL IRRVLAPAVR VHPGPPPANI KEITIRTPGS KSISNRALIL AALGNGTCRL
KNLLHSDDTQ VMINALEEMK GASFSWEDNG ATLVVSGGAG KLSSPANGKH VYLGNAGTAA
RFLTTVCSLV KSQVSNQSST VITGNARMQE RPIGPLVDTL RTNGVQIDYL RNEGCLPLRI
SPEDGFPGGM IELAASVSSQ YVSSVLLSAP FAQAPVTLSL VGVERVKDPA TGLPSNTYRI
PNGTYKNPPV YEIESDASSA TYPLAMAALN GLSITLETIG SGSLQGDAQF AKKVLEPMGC
QVIQTERETK VIGPSTVSEL RQLGEIDMEE MTDAFLTACV VLGVAVQPSE KEQKMSTRII
GIANQRVKEC NRIAAMVAEL GKMGIHAQEL EDGIEVFGTP VDALAKRGDQ VRINCYDDHR
IAMAFSVLGT VPGGKGLILN EKRCVEKTWP SWWDDLSTKL GIQLDGVPAH EKLTNTTSAV
AWEAKKPETP SILLCGMRGS GKSFSGQVAA STLGWPLIDT DLYFQEKCGC SIREFIQKND
WSRFREEECA VLEEILKEFP SCHVISLGGG IVETEKGRKM LMNYANSKGP VVEIIRPVEE
VIAYLNEDGN RPSLGESIQQ IWARREPWYR LCSNSEYFNL VHPAVDHALI SEVQHAKRAM
QQFFRFITGV DTNHVLLDPP VPRNTHFLCL TFPSLSPCRE EDKTSLDRFE ELTIGCDAVE
LRVDLLSTSG KAPTSPSIPP TEFVVKQVAA LRRLTTLPII YTVRTCSQGG MFPDGQPEEW
CKLAAMGFRT GCEYVDIELG LSPEQQKALC SQKGHSKIIA SYHDFSGRLK WDSSEMIQRY
HELKAYGDMV KLVSRAADGL EDNLAMLEFR KKHATLQKDR QSLITINMGR SGQMSRILSP
VLSPTTHRLL PGPPAAPGQL SFRQIQTAQG LLGQIIPKQF WLFGAPIGQS RSPLIHGTGF
DTLGLEGYRY QKCETSSVTD STVLEKIHAS DFGGASVTIP LKVEIIKYLD QLTPDAQAVG
AVNTIVPVSQ RDGKIKLLGA NTDWEAIKMK IEANLPAQQA LGLITPGQLV RAAGVVIGAG
GTARAAVYAL HSLGYEQIYI HNRTRSKAEE VAQAFPSYFG IRVIDSLGFL CSGEDGVWQP
SAIISAVPAQ ATRLSDDPPA DKLEIPHGLF DRPGGGVVIE MSYALGKDSA LLRAVQDLVR
WKSVDGLQVL VQQAARQFQL WTGKHLAMKI VSQAVYQEAS SD


Related products :

Catalog number Product name Quantity
AS14 2782 rabbit polyclonal EPSP synthase | 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic 50
EIAAB38426 Homo sapiens,Human,N-acetylneuraminate synthase,N-acetylneuraminate-9-phosphate synthase,N-acetylneuraminic acid phosphate synthase,N-acetylneuraminic acid synthase,NANS,SAS,Sialic acid synthase
EIAAB11775 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Homo sapiens,Human,Mannose-P-dolichol synthase,MPD synthase
EIAAB11776 Bos taurus,Bovine,Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Mannose-P-dolichol synthase,MPD synthase
EIAAB11774 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,Dpm1,Mannose-P-dolichol synthase,Mouse,MPD synthase,Mus musculus
orb60918 Shikimic acid Shikimic acid(Shikimate), more commonly known as its anionic form shikimate, is an important biochemical intermediate in plants and microorganisms. For research use only. 10 mg
EIAAB11773 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Mannose-P-dolichol synthase,MPD synthase,Pig,Sus scrofa
EIAAB06601 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,Homo sapiens,Human
EIAAB06600 Bos taurus,Bovine,CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,
EIAAB06597 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,CDS,CDS 1,CDS1,CTP phosphatidate cytidylyltransferase 1,Homo sapiens,H
EIAAB06603 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,Cds2,CTP phosphatidate cytidylyltransferase 2,Mouse,Mus musculus
EIAAB06599 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,Cds,CDS 1,Cds1,CTP phosphatidate cytidylyltransferase 1,Mouse,Mus musc
E0167h ELISA Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandi 96T
E0167h ELISA kit Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostag 96T
EIAAB28570 (2-5')oligo(A) synthase 1B,2-5A synthase 1B,2'-5'-oligoadenylate synthase 1B,2'-5'-oligoadenylate synthase-like protein 1,Mouse,Mus musculus,Oas1b,Oias2
63959-45-5 Shikimate-3-phosphate S-3-P 1g
U0167m CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167m ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167r ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
E0167b ELISA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167b ELISA kit Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167m ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167r ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
U0167b CLIA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
U0167r CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T


 

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