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

 A0A0D0AM01_9HOMO        Unreviewed;      1590 AA.
A0A0D0AM01;
29-APR-2015, integrated into UniProtKB/TrEMBL.
29-APR-2015, sequence version 1.
22-NOV-2017, entry version 26.
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=CY34DRAFT_804457 {ECO:0000313|EMBL:KIK42886.1};
Suillus luteus UH-Slu-Lm8-n1.
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Agaricomycetes; Agaricomycetidae; Boletales; Suillineae; Suillaceae;
Suillus.
NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485};
[1] {ECO:0000313|EMBL:KIK42886.1, ECO:0000313|Proteomes:UP000054485}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK42886.1,
ECO:0000313|Proteomes:UP000054485};
DOE Joint Genome Institute;
Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S.,
Martin F., Nordberg H.P., Cantor M.N., Hua S.X.;
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Proteomes:UP000054485}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
DOE Joint Genome Institute;
Mycorrhizal Genomics Consortium;
Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
"Evolutionary Origins and Diversification of the Mycorrhizal
Mutualists.";
Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
-!- 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:SAAS00858949}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00629607}.
-!- 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:SAAS00858971}.
-!- 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:SAAS00629576}.
-!- 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:SAAS00629599}.
-!- 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}.
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EMBL; KN835227; KIK42886.1; -; Genomic_DNA.
EnsemblFungi; KIK42886; KIK42886; CY34DRAFT_804457.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000054485; 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; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniPathway.
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_00110; DHQ_synthase; 1.
HAMAP; MF_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00222; Shikimate_DH_AroE; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR016037; DHQ_synth_AroB.
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; IPR010110; Shikimate_DH_AroM-type.
InterPro; IPR022893; Shikimate_DH_fam.
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; TIGR01357; aroB; 1.
TIGRFAMs; TIGR01093; aroD; 1.
TIGRFAMs; TIGR01809; Shik-DH-AROM; 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:SAAS00858978};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Complete proteome {ECO:0000313|Proteomes:UP000054485};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629621};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629772};
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:SAAS00629584};
NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172};
Reference proteome {ECO:0000313|Proteomes:UP000054485};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712179}.
DOMAIN 80 363 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 417 845 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1307 1388 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 1424 1476 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 46 48 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 84 87 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 115 117 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 140 141 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 180 183 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 884 891 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 389 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 195 198 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 269 273 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1302 1590 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 265 265 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 280 280 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 833 833 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1191 1191 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1219 1219 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 195 195 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 276 276 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 292 292 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 120 120 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 131 131 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 147 147 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 153 153 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 162 162 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 163 163 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 191 191 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 255 255 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 276 276 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 292 292 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 361 361 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1590 AA; 170223 MW; EF30A9B7658682A2 CRC64;
MDTVPDILKV SILGRESIHC GFHLIPYIAH TVLTTLPASV YVLVTDTNVA QFYLSAFEKA
FSAEISKLSS AKPRFLSRVI FPGETTKSRE GKADIEDFLL LERCTRDTVI LALGGGVIGD
LVGFVAATFM RGVRFVQIPT TLLAMVDSSV GGKTAIDTPA GKNLIGAFWQ PEYIFIDAAF
LESLPEREFS NGMAEVVKTA AIWDETEFTS LESNAQLIYN AIRTPSTGNA GRHISTRSTS
QSLLLSVIRG SIYVKSHIVT IDERETGLRN LVNFGHTIGH AIEAVLTPHM LHGECVSIGM
IFEAEVSRAM GILKQVAVGR LVRCLRAYGL PVSLADQRVT RCPGARGLGV DRLLDIMRVD
KKNSGPQKKV VILSSIGATY EQKATAVDDA LIAKVLSEAV TVKVDLSTTS GIQHVKMATP
GSKSISNRAL VLAALAQGTC RLKNLLHSDD TQVMMAALQE LKGASFAWED GGETLVVTGG
AGSLEVPTAG KEIYLGNAGT AARFLTTVCS LVSPSAAPDA GTATIITGNA RMKQRPIGPL
VDALRANGSE ITYNESEGCL PLSIAPKGLQ GGVIRLAASV SSQYVSSILL CAPYAREAVT
LELVGGAVIS QPYIDMTIAM MRTFGVLVTR DPGTDVYRIP QGTYVNPAQY AIESDASSAT
YPLAIAAITG TKCTLENIGS ESLQGDARFA VDVLARMGCE VVQTANETTV TGPKRGELKA
IGEVDMEPMT DAFLTACALA AVAQGGEGNT TRILGIANQR VKECNRIKAM IDQLAKFGVQ
TKELDDGLEV YGCPFNTLTR GASVHCYDDH RVAMAFSVLG TVVPDTIIEE KRCVEKTWPN
WWDDLENKIG LKVGGIELPR AEGSNTATSG TPSPAASASV ILIGMRGSGK SHIGKLASAA
LSRQFIDADI YFETKHNIGV REFVSVNGWP AFRAAETELL KEIIQKAGTG HVISMGGGIV
ETPQARDVLK DYAKTGPVVH VLRDIEEIVN YLGDETARPA YGEPITEVFK RREPWFIECA
NYDFVNHITV GDSEATNSEI SRFFKHITGQ PNLSENVAAG KRSYFVALTY PDVIPALRHM
SDLTTGVDAV ELRVDLLRAH NALGAIPSQA YVTAQLAALR RATSLPIIFT VRTISQGGAF
PDNSERDAFE LLALALRLGV EYIDVEISAS ERLITELAAR KGFSQIIASW HDWSGKMKWN
EDVVRSKYTL ASRFGDIVKI VGKADTLQDN FVLHDFVAKA NLQRGAKPII AINMGVEGQM
SRILNATLSP VTHPLLPSKA APGQLSFAQI QKALNLLGQL PAKRYFLFGN PIAHSMSPTL
HNTGFEVLGL PHTYELLETA SVGEELKATL AAPDFGGASV TIPFKLDVIP LLDKLSPAAE
AIGAVNTIIP VIEEGNRILY GDNTDWLGIR ESIRSRAPSI GAPAAALVIG AGGTARAAIF
ALQSLGAQRI YLFNRTASKA QALVDAFPDA PVKLIETLDV WPAEGPAPTV IVSTVPASAT
TTDGTSPGAV LLPLALFDAT ANGVVVDMAY KPAETPLLTL AKSAAPKWAR VMGVEVLLEQ
GYVQFETWTG RRCPKHVVSK SVLEKYFAAA


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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


 

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