ID A0A0L7QZK0_9HYME Unreviewed; 397 AA.
AC A0A0L7QZK0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Prostaglandin E synthase 2 {ECO:0000313|EMBL:KOC63967.1};
GN ORFNames=WH47_01282 {ECO:0000313|EMBL:KOC63967.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC63967.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC63967.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC63967.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549}.
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; KQ414681; KOC63967.1; -; Genomic_DNA.
DR RefSeq; XP_017791567.1; XM_017936078.1.
DR AlphaFoldDB; A0A0L7QZK0; -.
DR STRING; 597456.A0A0L7QZK0; -.
DR EnsemblMetazoa; XM_017936078.1; XP_017791567.1; LOC108573615.
DR GeneID; 108573615; -.
DR OrthoDB; 1226at2759; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; IEA:UniProtKB-EC.
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; IPR002109; Glutaredoxin.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
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; PF00462; Glutaredoxin; 1.
DR SFLD; SFLDG01182; Prostaglandin_E_synthase_like; 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.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 114..161
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 397 AA; 46148 MW; 8BB808AB01E82A59 CRC64;
MPILQRLSKL PRNLYSFKNI IQKYPKRNES FLSTSRQSSR LKTVLKASLI GISVGFPVGV
VITISYSWYV NKEASKTYHL QGKVQKIEIL KEKPQVPVSR KVVSPVDTTE LKLTLFQYQT
CPFCCKVRAF LDYYGISYDI VEVDPVLRKE ISWSSYKKVP ILLTQVESGY LPLNDSSMII
SLLASHLKDR SQNINDLIEC YPNIAMHDEN QKLKYEIMNK YFLMYKDTLL SVKNTDAIIE
ERKWRKWADD ELVHALSPNV YRTLDEAYNT FNWFSKVGNW EQYFPTWERL IMINVGATAM
WIISKRLKKR HNLKDDVRQS LYDEINKWLC AIKKRGSTFM GGEKPNLSDL AVYGILKSIE
GCSAFKDCLD NTKLSTWYDA MMTEIETRSG SKYLTAK
//
