ID T1G3D5_HELRO Unreviewed; 373 AA.
AC T1G3D5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Prostaglandin E synthase 2 {ECO:0000256|ARBA:ARBA00019474};
DE EC=5.3.99.3 {ECO:0000256|ARBA:ARBA00012203};
DE AltName: Full=Microsomal prostaglandin E synthase 2 {ECO:0000256|ARBA:ARBA00031041};
GN Name=20215583 {ECO:0000313|EnsemblMetazoa:HelroP78591};
GN ORFNames=HELRODRAFT_78591 {ECO:0000313|EMBL:ESO04932.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP78591, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO04932.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP78591}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)-
CC heptadecatrienoate + malonaldehyde; Xref=Rhea:RHEA:48644,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:90694, ChEBI:CHEBI:566274;
CC Evidence={ECO:0000256|ARBA:ARBA00023930};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48645;
CC Evidence={ECO:0000256|ARBA:ARBA00023930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023931};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894;
CC Evidence={ECO:0000256|ARBA:ARBA00023931};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004702}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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DR EMBL; AMQM01003983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB096411; ESO04932.1; -; Genomic_DNA.
DR RefSeq; XP_009016865.1; XM_009018617.1.
DR AlphaFoldDB; T1G3D5; -.
DR STRING; 6412.T1G3D5; -.
DR EnsemblMetazoa; HelroT78591; HelroP78591; HelroG78591.
DR GeneID; 20215583; -.
DR KEGG; hro:HELRODRAFT_78591; -.
DR CTD; 20215583; -.
DR eggNOG; KOG3029; Eukaryota.
DR HOGENOM; CLU_011226_0_1_1; -.
DR InParanoid; T1G3D5; -.
DR OMA; MSCFRLA; -.
DR OrthoDB; 1226at2759; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IBA:GO_Central.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03197; GST_C_mPGES2; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 6.20.200.30; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR034334; PGES2.
DR InterPro; IPR034335; PGES2_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12782; MICROSOMAL PROSTAGLANDIN E SYNTHASE-2; 1.
DR PANTHER; PTHR12782:SF5; PROSTAGLANDIN E SYNTHASE 2; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 51..123
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13417"
SQ SEQUENCE 373 AA; 42751 MW; E53660095F5FBE3B CRC64;
MLYFYYNNSA DEHTIRALSS PPHTIDKKTS IKVTKRIRSN TDNNHNLKLT LYQYQSCPFC
CKVRAYLDFK GLSYDIVEVN SVTQKEIKWS SYKKVPILSC RIGDKEEVQL NDSSVIISCL
ETYFLEKPPN QSIEKVALYY PSYEVKNVKG KMVMQFENKY SIMYGADKKV PDDQQKVQRW
REWTDNMLVH RISPNIYRSP MEAYDTFQVF AKEIFGTFHT NLIVIVGSAA MYFVGKILKR
RHKLPDDVRD SLYEACNEWC RNISSTDKTS KEQKKDTIFS PKFTKNTTLE KEIFYGGKEP
NLADLAVYGV LNAMEGTAAF SDVLNHTPIA RWFYAVKSEI NSRAGKRLKD GDVDKYAGSD
DVIVGGKAGS SVG
//
