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

 A0A0L0P802_9ASCO        Unreviewed;      1566 AA.
A0A0L0P802;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
22-NOV-2017, entry version 23.
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};
Name=ARO1 {ECO:0000256|HAMAP-Rule:MF_03143};
ORFNames=QG37_00269 {ECO:0000313|EMBL:KNE02464.1};
[Candida] auris.
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora;
Clavispora/Candida clade.
NCBI_TaxID=498019 {ECO:0000313|EMBL:KNE02464.1, ECO:0000313|Proteomes:UP000037122};
[1] {ECO:0000313|Proteomes:UP000037122}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=6684 {ECO:0000313|Proteomes:UP000037122};
PubMed=26346253; DOI=10.1186/s12864-015-1863-z;
Chatterjee S., Alampalli S.V., Nageshan R.K., Chettiar S.T., Joshi S.,
Tatu U.S.;
"Draft genome of a commonly misdiagnosed multidrug resistant pathogen
Candida auris.";
BMC Genomics 16:686-686(2015).
-!- 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KNE02464.1}.
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EMBL; LGST01000003; KNE02464.1; -; Genomic_DNA.
RefSeq; XP_018172187.1; XM_018309876.1.
EnsemblFungi; KNE02464; KNE02464; QG37_00269.
GeneID; 28874093; -.
KEGG; caur:QG37_00269; -.
KO; K13830; -.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000037122; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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_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.
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; 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:UP000037122};
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:UP000037122};
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 75 354 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 402 836 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1285 1366 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
DOMAIN 1403 1483 Shikimate_DH. {ECO:0000259|Pfam:PF01488}.
NP_BIND 81 84 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 112 114 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 137 138 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 177 180 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 874 881 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 380 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 192 195 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 258 262 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 863 1055 Shikimate kinase. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1280 1566 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 254 254 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 269 269 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 824 824 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1201 1201 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 192 192 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 265 265 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 281 281 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 117 117 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 128 128 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 144 144 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 150 150 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 159 159 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 160 160 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 188 188 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 244 244 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 265 265 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 281 281 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 352 352 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1566 AA; 171671 MW; 09FB6946C7CA0DC3 CRC64;
MAHVEKVTIL GSDSIHVGYG IQDHIVKETL QNLATSTYVI ITDENMEKTA PFRKLKASFE
AQIKEERPNS RLLSYAVSPG ENNKSRDTKA KVEDFLLLNG CTRDTVILAV GGGVVGDMIG
FVAATFMRGV RVVQVPTTLL AMVDSSVGGK TAIDTPLGKN FIGAFHQPKY VFVDVSFLET
LPTRQFINGM AEVVKTAAIW DEAEFTRLEN FASNFINVVT SDSIDLAEIK TDLVKTVLGL
IRVKAEVVSK DEKESSLRNL LNFGHTIGHA IEAIVTPQAL HGECVSIGMV LEAELSRYWG
ILSPVGVARL IKCLNAYNLP TSLDDKTFLL NVGFKRHLVV VDSVLKKMAV DKKNDGSKIR
TVILEAIGKC YQWKAHEVSR EDLRFVLTDE TLVKPFNPET TPATNTVIPP GSKSISNRAL
ILAALGLGTV KIKNLLHSDD TKHMLSAVSA LKGADIRTED NGETIVVTGN GGNLKTCDEQ
IYLGNAGTAS RFLTTVAALV NLNTDSGDHT ILTGNARMQE RPVGPLVDAL RSNGSDIEYL
NNEGSLPLKI KAGKGLKGGR IELAATISSQ YVSSILMCAP YADNEVTLAL VGGKPISQLY
IDMTISMMKS FGINVVKSTT EEHTYHIPKG VYKNPEVYEI ESDASSATYP LAFAAMTGTS
CTVPNIGSSS LQGDARFAVD VLKPMGCIVE QTSTSTTVKG PKRGTLKPLK HVDMEPMTDA
FLTASVVAAI ANDSTPTQIT GIANQRVKEC NRIKAMVDEL AKFGVTANEM PDGIEIYGVD
YKNLKAPLAE TGGVKTYDDH RVAMSFSLLA GMCSESVLIT ERSCTGKTWP GWWDVLHTNF
GVDLDGFEPP RDLNDISLLA NTAKNGDKSI IVIGMRAAGK STVSRWMAEL LGFDLIDADS
VFEEEHGDIR DFIKNESWQK FREIEANLLK KILSEKPTGH VISTGGGVVE SEECRALLKN
HKKTGIVLHL HRDLDETIVF LNSDATRPAY VSEVKDVWQR REKWYHECSN YLFYSAHCST
DNEFQKLRQS FANFIKTITG LETFKIPRDR TFAANLKLES YDGIVEALED ITAACSAVEI
RVDLLKDQTS SFVAEQVALL RKHISLPIIF TVRTRSQGGS FPDEDLETYQ ELTALAIKLG
VEFLDLQLNI PTVVTKKIFE KKGFTKIVAT YVDIHGKERW DEPAWDNRYN AAFSLNADVI
RLIGTAVNFQ ENILLENFRA SHQNTPLIAY NLGEQGKLSK MLNTIFTPVT SELMPGNASQ
EEVTVAEINS SLTLVGILNR KQFNVVGSPI EHSRSPDLHG SAYEALSLPY KFGRFESSNA
EEVYNELMKK PDFGGLAVTM PLKLDIMKFI DEFSDAAKLI GAVNTVVPLK GQPNKFFGDN
TDWYGITKSF SRNGVPSIEN SSVNGLVIGG GGTARAAAYA LHQLGCAKIY MINRTASKLH
DIVSLLPQEY NVEVLEMQEQ VAAAEPVSVA VSCVAADKPL DENLLDSVES LLQRGAKAKK
GGFNPTLLDA VYKPRVTPMM RIAQEKYQWT VVPGVEMLVN QGERQFQVHT GLTPPYKIIH
TAVVQE


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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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