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Pentafunctional AROM polypeptide [Includes: 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); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]

 A0A060S9A7_PYCCI        Unreviewed;      1616 AA.
A0A060S9A7;
03-SEP-2014, integrated into UniProtKB/TrEMBL.
03-SEP-2014, sequence version 1.
12-AUG-2020, entry version 51.
RecName: Full=Pentafunctional AROM polypeptide {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=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=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=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=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
ORFNames=BN946_scf184777.g13 {ECO:0000313|EMBL:CDO68983.1};
Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
Polyporales; Polyporaceae; Trametes.
NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO68983.1, ECO:0000313|Proteomes:UP000029665};
[1] {ECO:0000313|EMBL:CDO68983.1, ECO:0000313|Proteomes:UP000029665}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BRFM137 {ECO:0000313|EMBL:CDO68983.1,
ECO:0000313|Proteomes:UP000029665};
Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
Pontarotti P., Henrissat B., Record E.;
"The genome of the white-rot fungus Pycnoporus cinnabarinus: a
basidiomycete model with a versatile arsenal for lignocellulosic biomass
breakdown.";
Submitted (JAN-2014) 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}.
-!- CATALYTIC ACTIVITY:
Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- CATALYTIC ACTIVITY:
Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
ChEBI:CHEBI:145989; EC=2.5.1.19;
Evidence={ECO:0000256|ARBA:ARBA00001901, ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- CATALYTIC ACTIVITY:
Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+);
Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216;
EC=2.7.1.71; Evidence={ECO:0000256|ARBA:ARBA00000172,
ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- CATALYTIC ACTIVITY:
Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
Evidence={ECO:0000256|ARBA:ARBA00001648, ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- 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}.
-!- 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}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
4/7. {ECO:0000256|ARBA:ARBA00004871, 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
5/7. {ECO:0000256|ARBA:ARBA00004842, 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
6/7. {ECO:0000256|ARBA:ARBA00004811, ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514}.
-!- SIMILARITY: Belongs to the EPSP synthase family.
{ECO:0000256|ARBA:ARBA00009948}.
-!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}.
-!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase
family. {ECO:0000256|ARBA:ARBA00006477}.
-!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514}.
-!- SIMILARITY: In the 4th section; belongs to the type-I 3-dehydroquinase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514}.
-!- SIMILARITY: In the C-terminal section; belongs to the shikimate
dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514}.
-!- 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 shikimate kinase
family. {ECO:0000256|ARBA:ARBA00009349}.
-!- SIMILARITY: In the N-terminal section; belongs to the sugar phosphate
cyclases superfamily. Dehydroquinate synthase family.
{ECO:0000256|HAMAP-Rule:MF_03143}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation of
feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}.
-!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
whole genome shotgun (WGS) entry which is preliminary data.
{ECO:0000313|EMBL:CDO68983.1}.
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EMBL; CCBP010000030; CDO68983.1; -; Genomic_DNA.
EnsemblFungi; CDO68983; CDO68983; BN946_scf184777.g13.
HOGENOM; CLU_001201_1_2_1; -.
OrthoDB; 39786at2759; -.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000029665; 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_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|ARBA:ARBA00023141, ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
Rule:MF_03143};
Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
Rule:MF_03143};
NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03143};
Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
Rule:MF_03143};
Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
Reference proteome {ECO:0000313|Proteomes:UP000029665};
Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514}.
DOMAIN 72..357
/note="DHQ_synthase"
/evidence="ECO:0000259|Pfam:PF01761"
DOMAIN 409..850
/note="EPSP_synthase"
/evidence="ECO:0000259|Pfam:PF00275"
DOMAIN 1331..1412
/note="Shikimate_dh_N"
/evidence="ECO:0000259|Pfam:PF08501"
DOMAIN 1448..1500
/note="Shikimate_DH"
/evidence="ECO:0000259|Pfam:PF01488"
NP_BIND 45..47
/note="NAD"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
NP_BIND 78..81
/note="NAD"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
NP_BIND 109..111
/note="NAD"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
NP_BIND 134..135
/note="NAD"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
NP_BIND 174..177
/note="NAD"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
NP_BIND 888..895
/note="ATP"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
REGION 1..383
/note="3-dehydroquinate synthase"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
REGION 189..192
/note="Substrate binding 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
REGION 263..267
/note="Substrate binding 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
REGION 1326..1616
/note="Shikimate dehydrogenase"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
ACT_SITE 259
/note="Proton acceptor; for 3-dehydroquinate synthase
activity"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
ACT_SITE 274
/note="Proton acceptor; for 3-dehydroquinate synthase
activity"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
ACT_SITE 838
/note="For EPSP synthase activity"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
ACT_SITE 1215
/note="Proton acceptor; for 3-dehydroquinate dehydratase
activity"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
ACT_SITE 1243
/note="Schiff-base intermediate with substrate; for 3-
dehydroquinate dehydratase activity"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
METAL 189
/note="Zinc; catalytic"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
METAL 270
/note="Zinc; catalytic"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
METAL 286
/note="Zinc; catalytic"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 114
/note="NAD"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 125
/note="Substrate 1"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 141
/note="Substrate 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 147
/note="Substrate 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 156
/note="NAD"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 157
/note="Substrate 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 185
/note="NAD"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 249
/note="Substrate 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 270
/note="Substrate 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 286
/note="Substrate 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
BINDING 355
/note="Substrate 2"
/evidence="ECO:0000256|HAMAP-Rule:MF_03143"
SEQUENCE 1616 AA; 175362 MW; A9970A22DD825B2D CRC64;
MAHVDVRKVS ILGKESIHCG FHLISYIVET VTKTLPSSTY VLVTDTNVGN LYVPAFQTEF
DARKGQARFL TYVVAPGETS KSREGKAEIE DFLLLNKCTR DTVILALGGG VIGDLVGFVA
ATFMRGVRFV QIPTTLLAMV DSSVGGKTAI DTPHGKNLIG AFWQPEYIFI DAAFLETLPA
REFSNGMAEV IKTAAIWDEK EFASLESRAA EIFAAIQTPS VNFAGRTEST RSPAQQLLLS
VIAGSIGVKA HIVTIDERET GLRNLVNFGH TIGHAIEAVL TPAMLHGECV AVGMVLEAEV
ARQLGVLSQV AVGRLTRCLK AYNLPVSLSD PRISSLPTAR SLSVSKLLDI MKIDKKNSGP
QKKIVILSRI GATYEPKATV VADKVIAKTL SEAVKVVPGT PSKSPIRMAT PGSKSISNRA
LLLAALGTGT CRLKNLLHSD DTQVMMNALV ELQGAKFDWE DGGETLVVNG GAGALSVPRD
GKEIYLGNAG TAARFLTTVC TLVQTQSSGQ RTVITGNARM KQRPIGPLVD ALRANGSSIE
YLESQGCLPL SIAPAGLKGA HIQLAASVSS QYVSSILLCA PYAAEPVTLE LTGGQVISQP
YIDMTIAMMK TFGIEVVRES DPQTGKLLDV YRIPKGVYRN PVEYNIESDA SSATYPLAIA
AITGTTCTIT NIGSASLQGD ARFAKEVLEP MGCKVIQTET ETTVTGPPVG QLRALGLVDM
EPMTDAFLTA SVLAAVATRP PLPERTLQDG SNPNTTRIIG IANQRVKECN RIKAMIDELA
KFGVETLELD DGLEVYGKPI EELKQGVSVH CYDDHRVAMA FSVLGSIIKE TIIEEKRCVE
KTWPNWWDDL ENKIGLEVEG VELSFIHGAA SASRPTDDSS RASVVLIGMR GSGKTFIGKL
AASTLRWQFV DADAYFEQKH QIGVREFVQK NGWSAFREAE TEILKELLEQ NGREHVISLG
GGIVETPTAR DILKAYTQKG PVVHIVREID EVISYLGEET ARPGYGEPVI DVFKRRAPWF
AECCSYEFVN YTGVLTSSGA LAENDTKAAP SLLSVRDEVS RFFNHITGQR PNLAPNLAKG
KRSYFLCLTY PDITPALPYV QDMAAGVDAI EVRVDLLRSP KDFDKLGPYV PSTNYVTEQI
TALRHKTSVP LIFTVRTVSQ GGQFPDHSEK EAFELFFTAV RLGVEYIDVE ISWSEKNIQD
LIAHKGHSQI IASWHDWSGN MHWDSKLVEA KYHAAHDIGD IVKLVGKANG LEDNFALHNF
VLRMQAARDA KPIIAINMGV EGQMSRILNS TFSPVTHPLL PSKAAPGQLS FAQIQTALHL
LGQLPAKKFY LFGNPIAHSM SPTLHNTAFE ALGLPHKYEL LQTEAVGEEI KTAVTSPDFG
GASVTIPFKR DIMPLLDALS EDAEAIGAVN TVIPRKREDG SLMLYGDNTD WRGILQSIRR
SLPQSILQPE AALVIGAGGT SRAAIYALWK LGVKNVYLFN RTRTSAETLV ATFPEVHIKL
VDELGVWPND GPAPTVIVST VPASATSLDR FATDTLYLPA SLFAASTGGV VIDMAYKPAE
TPLLALAMNV GKNWRTVMGV EVLLEQGYDQ FHLWTGRHCP KGIVSDRVWQ VYSMSA


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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