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

 R4XAX9_TAPDE            Unreviewed;      1604 AA.
R4XAX9;
24-JUL-2013, integrated into UniProtKB/TrEMBL.
24-JUL-2013, sequence version 1.
25-APR-2018, entry version 46.
RecName: Full=Pentafunctional AROM polypeptide {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 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 dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {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};
ORFNames=TAPDE_002851 {ECO:0000313|EMBL:CCG82719.1};
Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI
108563 / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria
deformans).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Taphrinomycetes; Taphrinales; Taphrinaceae; Taphrina.
NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG82719.1, ECO:0000313|Proteomes:UP000013776};
[1] {ECO:0000313|EMBL:CCG82719.1, ECO:0000313|Proteomes:UP000013776}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
PubMed=23631913; DOI=10.1128/mBio.00055-13;
Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
Overmyer K., Hauser P.M., Pagni M.;
"Genome sequencing of the plant pathogen Taphrina deformans, the
causal agent of peach leaf curl.";
MBio 4:E0005513-E0005513(2013).
-!- 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|PIRNR:PIRNR000514,
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|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858949}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629607}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712174}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:CCG82719.1}.
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EMBL; CAHR02000097; CCG82719.1; -; Genomic_DNA.
OrthoDB; EOG092C02JU; -.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000013776; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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_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; IPR000623; Shikimate_kinase/TSH1.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 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.
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:UP000013776};
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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000013776};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712179}.
TRANSMEM 110 131 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 80 358 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 427 848 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1310 1390 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
NP_BIND 42 44 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 85 88 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 116 118 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 141 142 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 181 184 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 880 887 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 384 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 196 199 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 264 268 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1305 1604 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 260 260 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 275 275 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 836 836 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1195 1195 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 196 196 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 271 271 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 287 287 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 121 121 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 132 132 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 148 148 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 154 154 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 163 163 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 164 164 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 192 192 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 250 250 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 271 271 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 287 287 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 356 356 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1604 AA; 175310 MW; A4FE4B9966E67B47 CRC64;
MSITKVKILG KESIHVGYNL IPHIVDTCLS ELPSSTYVVI TDTNIAPLYL DQFSDHMKQS
IQDRQRFPSL PNQSRFLAKV ISPGETSKSR ETKADLEDWM LSHRCTRDTV VIALGGGVIG
DMIGFVAATF MRGVKFVQVP TTLLAMVDSA IGGKTAVDTF LGKNLIGAFH QPEFIFEDLS
FLNTLPNREF INGMAEVIKT AAIWREDKFA LLERSATLIL EILSQPVSAH RFDGIRELLQ
DVVISSILVK AEVVSADEKE GGLRNLLNFG HSIGHAYEAI LTPEILHGEA VSIGMIKEAE
LSRYLGHLAP EAVGRLSKCL SAWGLPTSVH DKFITSKTGG RPTELENLLD IMAVDKKNAG
RMKKIVLLKK IGQCVEMKAT NVPDEHIRLV LAPHVFVHNS NTSNSSSMNG NTTGSQTKGT
DRRVVCRPPG SKSISNRAMI LAALSGGTTR LTNLLSSDDT RYMQTALEML GAASFSWKDD
GSLEVRGTGQ FSNPGKGKEI FLGNAGTAAR FLTSVVTLVG GSDPITVTGN ERMKVRPIGP
LVDALRANGS TIKYLANDGC LPLSVQPGFR GGRIELSAKV SSQYVSSLLM IAPLAQEPVH
LFLTGDKVIS ELYIDMTTAM MATFGITVEK VSSSEYKIPL GKYHAPEQYE IESDASSSTY
PLALAALLGI EVHVPNIGSD SLQGDARFAK DVLEPMGCTV KQTSSSTTVQ GPPRGELRAI
KTVDMEPMTD AFLTATVLAA VTNSDMSITG IANQRVKECN RIVAMMTGLR RFGVTNTSEL
PDGLIIHGVG YDGLKAPVAN YVHDGVDTYD DHRVAMSFSL LGAVTPGKSL ILDKACTSKT
WPDWWDVLSH DFGITLTGQD ELPEKPRASI NGESSVLVVG MRGAGKTTMG RLAAKILGRP
FIDLDDMLEQ DYGRRIPLIT ETDGWPAFRE MELATLKKFI QTKSLGWVAA CGGGVVETPA
AVKILEEYSA AGGIVLQVHR DVDKIVEFLG EDKTRPAWNK AQGSSRSEIL GVWKRRQPAF
ERVSNFQYYS TDTTSQVMMP RQANAYARFL RHIQGREDNH TRLTKKPRTY FLSLTHPDVR
DALQYLDTVA AGCDAVELRV DLLRENNEDY PSIAYVSEQI AILRDHSDLP IIFTIRSRDQ
GGRFPNKRED KALELMLIAS KWGVEYIDFE ITWSDLMLRE VRRYAVCSKI IASYHDVSGN
LSFNSATWRT RYDRARQIGD VVELIGRANH LEDNFALEHF RTELSREDHP PIIMINMGAE
GKLSRILNTF LTPITHELFP VKAAPGQLSL HEVNTGLSLI GELKPKQYFI FGTPISHSRS
PALHNTGFAS FGLPHVYSRM ESINIQDYAT ILQSDDFGGA SVTIPHKQAI MPFLSEISEE
ATEIGAVNTV IPLPGGGLRG DNSDWIGIMR SLMNYSNIAA DGASGVVLGA GGTARAAIYA
LKRLNVGKIY LANRSRKNLD ALIKAFPFVV PIASAEEASA IDRPCVAVST VPGDGPLDPT
IASIAAAVFA RGVSAPTLLE MAYKPKVTPM MQLAMEARWK TIEGLEPLVE QGLRQFSLWT
GFDMSVVQAR QAVLGEEVTT IPVTSGQPYY KKAVEGVWQS VVES


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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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