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Database: UniProt
Entry: A1Y2D3_LEIIN
LinkDB: A1Y2D3_LEIIN
Original site: A1Y2D3_LEIIN 
ID   A1Y2D3_LEIIN            Unreviewed;       273 AA.
AC   A1Y2D3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Prostaglandin f2-alpha synthase {ECO:0000313|EMBL:ABI17865.1};
DE   Flags: Fragment;
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:ABI17865.1};
RN   [1] {ECO:0000313|EMBL:ABI17865.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bman {ECO:0000313|EMBL:ABI17866.1}, LIU
RC   {ECO:0000313|EMBL:ABL10356.1}, and OG-VL
RC   {ECO:0000313|EMBL:ABI17865.1};
RX   PubMed=17142569; DOI=10.1128/EC.00282-06;
RA   Waki K., Dutta S., Ray D., Kolli B.K., Akman L., Kawazu S., Lin C.P.,
RA   Chang K.P.;
RT   "Transmembrane molecules for phylogenetic analyses of pathogenic protists:
RT   Leishmania-specific informative sites in hydrophilic loops of
RT   trans- endoplasmic reticulum N-acetylglucosamine-1-phosphate transferase.";
RL   Eukaryot. Cell 6:198-210(2007).
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DR   EMBL; DQ834276; ABI17865.1; -; Genomic_DNA.
DR   EMBL; DQ834277; ABI17866.1; -; Genomic_DNA.
DR   EMBL; DQ981498; ABL10356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1Y2D3; -.
DR   VEuPathDB; TriTrypDB:LINF_310029700; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43827; 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE; 1.
DR   PANTHER; PTHR43827:SF3; ALDO-KETO REDUCTASE; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   4: Predicted;
FT   DOMAIN          14..264
FT                   /note="NADP-dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00248"
FT   ACT_SITE        48
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT   SITE            73
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABI17865.1"
FT   NON_TER         273
FT                   /evidence="ECO:0000313|EMBL:ABI17865.1"
SQ   SEQUENCE   273 AA;  30588 MW;  31B0143CA163BB04 CRC64;
     PMVTLSNGVQ MPQLGLGVWQ SPAGEVTANA VKWALCAGYR HIDTAAIYKN EESVGAGLRA
     SGVPREDVFI TTKLWNTEQG YESTLAAFEE SRQKLGVDYI DLYLIHWPRG KDIVSKEGKK
     YLDSWRAFEQ LYKDKKVRAI GVSNFHIHHL EDVLAMCTVT PMVNQVELHP LNNQAELRAF
     CDAKQIKVEA WSPLGQGKLL SNPILAAIGA KYNKTAAQVI LRWNIQKNLI TIPKSVHKER
     IEENADVFNF ELGAEDVMRI DALNTNSRYG PDP
//
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