ID A0A498I053_MALDO Unreviewed; 1076 AA.
AC A0A498I053;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ORFNames=DVH24_023502 {ECO:0000313|EMBL:RXH77228.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH77228.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH77228.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH77228.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH77228.1}.
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DR EMBL; RDQH01000340; RXH77228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498I053; -.
DR STRING; 3750.A0A498I053; -.
DR EnsemblPlants; mRNA:MD14G0205600; mRNA:MD14G0205600; MD14G0205600.
DR EnsemblPlants; mRNA:MD14G0205700; mRNA:MD14G0205700; MD14G0205700.
DR Gramene; mRNA:MD14G0205600; mRNA:MD14G0205600; MD14G0205600.
DR Gramene; mRNA:MD14G0205700; mRNA:MD14G0205700; MD14G0205700.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000290289; Chromosome 14.
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; cd04038; C2_ArfGAP; 1.
DR CDD; cd03197; GST_C_mPGES2; 1.
DR CDD; cd03040; GST_N_mPGES2; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46310; AMIDASE 1; 1.
DR PANTHER; PTHR46310:SF5; OUTER ENVELOPE PROTEIN 64, CHLOROPLASTIC; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS50404; GST_NTER; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
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:ARBA00023160};
KW Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1076
FT /note="Prostaglandin E synthase 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019799602"
FT DOMAIN 100..176
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT REPEAT 861..894
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 900..1015
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1076 AA; 118387 MW; 077B6DFD57734CCB CRC64;
MRRASTLASL PLLSRSLSTA HGGAAVTSAP TTYGLLQVAL YGTTSTGSQV PRRWLDSFYG
GSGRKLAIGV AGTLASVAVA TSLAPEVYAK EPPPAALVPK EVVLYQYEAC PFCNKVKAFL
DYHDIPYKVV EVNPLSKKEI KWSDYQKVPI LMVDGEQLVD SSAIIDQLNS KIVPERSAAS
SSDDDEEKKW RQWVDNHLVH MLSPNIYRNT SEALESFDYI TSNGNFSYTE KISVKYAGAA
AMYFVSKKLK KKYNITDERA SLYEAAETWV DALNGRDFLG GSKPNLADLA VFGVLRPIRY
LRSGKDMVEH TRIGEWYSRM ERAAANLWVL LGLGLAGILL MTRKLKKTIR EDFGAFVERL
QLLPPPQPAP PKAPHPLTGL TFAVSDVFEI EGHVTGFGHP DWGRTHDAAS RTCPVVSTLV
EGGATCTGIT VVDELAYSIT GENKHYGTPT NPAASSRKPG GSSSGAAVAV AADLVDFSLG
LDTVGGVRVP AGSCGIIGFR ASHGSVSHAG FIPVSTSLDT VGWFARDPNV LRRVGHVLLQ
LPYAVSRSPR QIVIADDCFQ EVKIPVDRIV QVVIKSTEKL FGKQVLKHEN IGDYCNSKVP
SLKKFHGLKT NGEVKTSSLK LLANVVQFLQ RHEFRHNHGE WIDSVKPVLE SATSAQICGP
LEASDEEIEI CKSIRNELRA AVSSLLKDDG ILVIPTIADP PAKLGGKEML SEDFRNRTFG
LLSIASLSGC CQVTAPLGFY DKCPVSVSFI ARHGGDRFLL DALHTMYMSL QEQADIASKS
RSSKNALTKE QSAEIAKEKG NQAYKDREWQ KAIGFYSEAI KLSGNNATYY SNRAQAYLEV
GSFIQAEADC TKAINLDKKN VKAYFRRGTA REMLGYYKEA IEDFRHTLVL EPTNKRAAVA
AEKLRKLFLK SLMENLLGLL RIRVKRGVNL AVRDVRSSDP YVVIKMGKQK LKTRVIKKDI
NPEWNEDLTL SITDPSIPIK LTVFDHDTFS KDDKMGDAEF GISPYLEALK MNLEGVPSGT
TVSRIQPDRA NCLAEESCIQ WKDGKVVQDM CLRLRNVECG EVEVQLQWID LPVIII
//
