PGFS_TRYCC
ID PGFS_TRYCC Reviewed; 283 AA.
AC Q4DJ07;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=9,11-endoperoxide prostaglandin H2 reductase {ECO:0000305};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q9GV41};
DE AltName: Full=Prostaglandin F2-alpha synthase;
GN ORFNames=Tc00.1047053511287.49;
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener;
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RC STRAIN=CL Brener;
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "crystal structure of prostaglandin F synthase from Trypanosoma cruzi.";
RL Submitted (JUL-2012) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NADP-dependent formation of prostaglandin F2-
CC alpha from prostaglandin H2. Has also aldo/ketoreductase activity
CC towards the synthetic substrates 9,10-phenanthrenequinone and p-
CC nitrobenzaldehyde. {ECO:0000250|UniProtKB:Q9GV41}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC H2; Xref=Rhea:RHEA:45312, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:Q9GV41};
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9GV41}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GV41}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AAHK01000429; EAN92511.1; -; Genomic_DNA.
DR RefSeq; XP_814362.1; XM_809269.1.
DR PDB; 4FZI; X-ray; 2.60 A; A/B=1-282.
DR PDB; 4GIE; X-ray; 1.25 A; A=1-282.
DR PDBsum; 4FZI; -.
DR PDBsum; 4GIE; -.
DR AlphaFoldDB; Q4DJ07; -.
DR SMR; Q4DJ07; -.
DR STRING; 5693.XP_814362.1; -.
DR PaxDb; Q4DJ07; -.
DR EnsemblProtists; EAN92511; EAN92511; Tc00.1047053511287.49.
DR GeneID; 3545874; -.
DR KEGG; tcr:511287.49; -.
DR eggNOG; KOG1577; Eukaryota.
DR OrthoDB; 1216642at2759; -.
DR BRENDA; 1.1.1.188; 6524.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0036130; F:prostaglandin H2 endoperoxidase reductase activity; IEA:RHEA.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.100; -; 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; PTHR43827; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NADP; Nucleotide-binding;
KW Oxidoreductase; Prostaglandin biosynthesis; Prostaglandin metabolism;
KW Reference proteome.
FT CHAIN 1..283
FT /note="9,11-endoperoxide prostaglandin H2 reductase"
FT /id="PRO_0000419494"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 53
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 23..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 140..141
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 188..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 234..236
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 240..244
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 78
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="V -> A (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="Y -> C (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="S -> N (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="R -> K (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..199
FT /note="EEAGI -> DRTGF (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 271..272
FT /note="GD -> AH (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:4GIE"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:4GIE"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:4GIE"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4GIE"
SQ SEQUENCE 283 AA; 32571 MW; F1D8D32017208BB8 CRC64;
MNCNYNCVTL HNSVRMPQLG LGVWRAQDGA ETANAVRWAI EAGYRHIDTA YIYSNERGVG
QGIRESGVPR EEVWVTTKVW NSDQGYEKTL AAFERSRELL GLEYIDLYLI HWPGKKKFVD
TWKALEKLYE EKKVRAIGVS NFEPHHLTEL FKSCKIRPMV NQVELHPLFQ QRTLREFCKQ
HNIAITAWSP LGSGEEAGIL KNHVLGEIAK KHNKSPAQVV IRWDIQHGIV TIPKSTNKGR
IQENFNVWDF KLTEEEMRQI DELNEDKRIG GDPDNFFPGG EEA
