ID PTGR1_PIG Reviewed; 329 AA. AC Q29073; O62642; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=Prostaglandin reductase 1; DE Short=PRG-1; DE EC=1.3.1.-; DE AltName: Full=NADP-dependent leukotriene B4 12-hydroxydehydrogenase; DE EC=1.3.1.74; DE AltName: Full=15-oxoprostaglandin 13-reductase; DE EC=1.3.1.48; GN Name=PTGR1; Synonyms=LTB4DH; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS RP OF ALA-149; ALA-150; GLY-152; GLY-155; GLY-159 AND GLY-166. RC TISSUE=Kidney; RX MEDLINE=96162034; PubMed=8576264; DOI=10.1074/jbc.271.5.2844; RA Yokomizo T., Ogawa Y., Uozumi N., Kume K., Izumi T., Shimizu T.; RT "cDNA cloning, expression, and mutagenesis study of leukotriene B4 12- RT hydroxydehydrogenase."; RL J. Biol. Chem. 271:2844-2850(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION. RC TISSUE=Lung; RX MEDLINE=98129716; PubMed=9461497; RA Ensor C.M., Zhang H., Tai H.-H.; RT "Purification, cDNA cloning and expression of 15-oxoprostaglandin 13- RT reductase from pig lung."; RL Biochem. J. 330:103-108(1998). RN [3] RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-15. RC TISSUE=Kidney; RX MEDLINE=93352633; PubMed=8394361; RA Yokomizo T., Izumi T., Takahashi T., Kasama T., Kobayashi Y., Sato F., RA Taketani Y., Shimizu T.; RT "Enzymatic inactivation of leukotriene B4 by a novel enzyme found in RT the porcine kidney. Purification and properties of leukotriene B4 12- RT hydroxydehydrogenase."; RL J. Biol. Chem. 268:18128-18135(1993). CC -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts CC on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity CC towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of CC leukotriene B4 into its biologically less active metabolite, 12- CC oxo-leukotriene B4. This is an initial and key step of metabolic CC inactivation of leukotriene B4. CC -!- CATALYTIC ACTIVITY: n-alkanal + NAD(P)(+) = alk-2-enal + NAD(P)H. CC -!- CATALYTIC ACTIVITY: 11-alpha-hydroxy-9,15-dioxoprost-5-enoate + CC NAD(P)(+) = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13- CC dienoate + NAD(P)H. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=7.7 uM for 15-oxo-PGE1; CC KM=19 uM for 15-oxo-PGE2; CC KM=10 uM for LTB4; CC KM=153 uM for NADH; CC KM=15 uM for NADPH; CC Vmax=2470 nmol/min/mg enzyme with 15-keto-PGE1 as substrate; CC Vmax=847 nmol/min/mg enzyme with 15-keto-PGE2 as substrate; CC Vmax=7.0 nmol/min/mg enzyme with LTB4 as substrate; CC Vmax=2352 nmol/min/mg enzyme with NADH as substrate; CC Vmax=729 nmol/min/mg enzyme with NADPH as substrate; CC -!- SUBUNIT: Monomer or homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Ubiquitously distributed in various tissues CC and leukocytes, the kidney and liver had the highest enzyme CC activities. CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D49386; BAA08381.1; -; mRNA. DR EMBL; U87622; AAC39170.1; -; mRNA. DR PIR; A47421; A47421. DR RefSeq; NP_999550.1; -. DR UniGene; Ssc.14490; -. DR SMR; Q29073; 1-329. DR GeneID; 397678; -. DR KEGG; ssc:397678; -. DR HOVERGEN; Q29073; -. DR BRENDA; 1.3.1.48; 249. DR BRENDA; 1.3.1.74; 249. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IEA:EC. DR GO; GO:0032440; F:2-alkenal reductase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002085; ADH_SF_Zn. DR InterPro; IPR013149; ADH_Zn-bd. DR InterPro; IPR014190; B4_12hDH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR TIGRFAMs; TIGR02825; B4_12hDH; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase. FT CHAIN 1 329 Prostaglandin reductase 1. FT /FTId=PRO_0000218067. FT NP_BIND 149 166 NADP (Potential). FT COMPBIAS 250 257 Pro-rich. FT BINDING 178 178 NADP (By similarity). FT BINDING 193 193 NADP (By similarity). FT BINDING 217 217 NADP (By similarity). FT BINDING 245 245 NADP (By similarity). FT BINDING 321 321 NADP (By similarity). FT MUTAGEN 149 149 A->E: Reduces activity by 90%. FT MUTAGEN 149 149 A->V: Reduces activity by half. FT MUTAGEN 150 150 A->V: No effect. FT MUTAGEN 152 152 G->V: Loss of activity. FT MUTAGEN 155 155 G->V: Reduces activity by 99%. FT MUTAGEN 159 159 G->V: Reduces activity by 60%. FT MUTAGEN 166 166 G->V: Reduces activity by 99%. FT CONFLICT 118 118 T -> A (in Ref. 2; AAC39170). SQ SEQUENCE 329 AA; 35762 MW; D8893061A7EFBEEA CRC64; MVRAKSWTLK KHFVGYPTPS NFELKTVELP PLKNGEVLLE ALFLTVDPYM RIAARKLKEG DMMMGEQVAR VIESKNAAFP TGTIVVALLG WTTHSISDGK NLERLLAEWP DTLPLSLTLG TVGMPGLTAY FGLLDICGLK GGETVMVNAA AGAVGSVVGQ IAKLKGCKVV GAAGSDEKVA CLKKYGFDVA FNYKTIESLE ETLKKASPEG YDCYFDNVGG EFSNAVTSQM KKFGRIAICG AISTYNRTGP PPPGPPPEVV IYNELCFQGF IVTRWQGEVR QKALRDLLKW VSEGKIQYHE HITEGFENMP AAFMGMLKGE NLGKAIVKA //