PGFS1_BOVIN
ID PGFS1_BOVIN Reviewed; 323 AA.
AC P05980;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Prostaglandin F synthase 1;
DE Short=PGF 1;
DE Short=PGF synthase 1;
DE Short=PGFS1;
DE EC=1.1.1.188;
DE AltName: Full=Prostaglandin F synthase I;
DE Short=PGFSI;
DE AltName: Full=Prostaglandin-D2 11 reductase 1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lung;
RX PubMed=2829166; DOI=10.1073/pnas.85.1.11;
RA Watanabe K., Fujii Y., Nakayama K., Ohkubo H., Kuramitsu S., Kagamiyama H.,
RA Nakanishi S., Hayaishi O.;
RT "Structural similarity of bovine lung prostaglandin F synthase to lens
RT epsilon-crystallin of the European common frog.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:11-15(1988).
CC -!- FUNCTION: Catalyzes the reduction of PGD(2) and PGH(2) to PGF(2 alpha)
CC and a stereoisomer, respectively. It has a broad substrate specificity
CC and reduces also other carbonyl compounds.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin
CC D2; Xref=Rhea:RHEA:10140, ChEBI:CHEBI:15378, ChEBI:CHEBI:57404,
CC ChEBI:CHEBI:57406, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.188;
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; J03570; AAA30694.1; -; mRNA.
DR PIR; A28396; A28396.
DR RefSeq; NP_001159696.1; NM_001166224.1.
DR AlphaFoldDB; P05980; -.
DR SMR; P05980; -.
DR PeptideAtlas; P05980; -.
DR GeneID; 782922; -.
DR KEGG; bta:782922; -.
DR OrthoDB; 1016440at2759; -.
DR SABIO-RK; P05980; -.
DR UniPathway; UPA00662; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0047023; F:androsterone dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0032052; F:bile acid binding; IBA:GO_Central.
DR GO; GO:0047086; F:ketosteroid monooxygenase activity; IBA:GO_Central.
DR GO; GO:0036131; F:prostaglandin D2 11-ketoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047017; F:prostaglandin-F synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016229; F:steroid dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0044597; P:daunorubicin metabolic process; IBA:GO_Central.
DR GO; GO:0044598; P:doxorubicin metabolic process; IBA:GO_Central.
DR GO; GO:0042448; P:progesterone metabolic process; IBA:GO_Central.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006693; P:prostaglandin metabolic process; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR CDD; cd19108; AKR_AKR1C1-35; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044482; AKR1C.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
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 Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; NADP;
KW Oxidoreductase; Prostaglandin biosynthesis; Prostaglandin metabolism;
KW Reference proteome.
FT CHAIN 1..323
FT /note="Prostaglandin F synthase 1"
FT /id="PRO_0000124646"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 20..24
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166..167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 216..221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 270..280
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 36720 MW; 27E35CA47FB2FECC CRC64;
MDPKSQRVKL NDGHFIPVLG FGTYAPEEVP KSEALEATKF AIEVGFRHVD SAHLYQNEEQ
VGQAIRSKIA DGTVKREDIF YTSKLWCNSL QPELVRPALE KSLQNLQLDY VDLYIIHSPV
SLKPGNKFVP KDESGKLIFD SVDLCHTWEA LEKCKDAGLT KSIGVSNFNH KQLEKILNKP
GLKYKPVCNQ VECHPYLNQS KLLEFCKSHD IVLVAYAALG AQLLSEWVNS NNPVLLEDPV
LCAIAKKHKQ TPALVALRYQ VQRGVVVLAK SFNKKRIKEN MQVFDFELTP EDMKAIDGLN
RNIRYYDFQK GIGHPEYPFS EEY
