ID A0A7J7BP38_9COLE Unreviewed; 333 AA. AC A0A7J7BP38; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 22-FEB-2023, entry version 9. DE RecName: Full=Prostaglandin reductase 1 {ECO:0000256|ARBA:ARBA00020651}; DE EC=1.3.1.48 {ECO:0000256|ARBA:ARBA00011981}; DE EC=1.3.1.74 {ECO:0000256|ARBA:ARBA00012410}; DE AltName: Full=15-oxoprostaglandin 13-reductase {ECO:0000256|ARBA:ARBA00033119}; DE AltName: Full=Dithiolethione-inducible gene 1 protein {ECO:0000256|ARBA:ARBA00032255}; DE AltName: Full=Leukotriene B4 12-hydroxydehydrogenase {ECO:0000256|ARBA:ARBA00031851}; DE AltName: Full=NAD(P)H-dependent alkenal/one oxidoreductase {ECO:0000256|ARBA:ARBA00032297}; GN ORFNames=FQR65_LT06766 {ECO:0000313|EMBL:KAF5307610.1}; OS Abscondita terminalis. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea; OC Lampyridae; Luciolinae; Abscondita. OX NCBI_TaxID=2069292 {ECO:0000313|EMBL:KAF5307610.1, ECO:0000313|Proteomes:UP000563990}; RN [1] {ECO:0000313|EMBL:KAF5307610.1, ECO:0000313|Proteomes:UP000563990} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ate-2015 {ECO:0000313|EMBL:KAF5307610.1}; RC TISSUE=Adult {ECO:0000313|EMBL:KAF5307610.1}; RA Zhang R., He J., Dong Z., Liu G., Yin Y., Zhang X., Li Q., Ren Y., Liu W., RA Chen X., Xia W., Duan K., Hao F., Lin Z., Yang J., Chang Z., Zhao R., RA Wan W., Lu S., Peng Y., Ge S., Wang W., Li X.; RT "Genomic and experimental data provide new insights into luciferin RT biosynthesis and bioluminescence evolution in fireflies."; RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate + CC NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate + CC H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974, CC ChEBI:CHEBI:133975; Evidence={ECO:0000256|ARBA:ARBA00023498}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51213; CC Evidence={ECO:0000256|ARBA:ARBA00023498}; CC -!- CATALYTIC ACTIVITY: CC Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin CC F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374, CC ChEBI:CHEBI:133409; Evidence={ECO:0000256|ARBA:ARBA00023548}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590; CC Evidence={ECO:0000256|ARBA:ARBA00023548}; CC -!- CATALYTIC ACTIVITY: CC Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15- CC oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:133408; CC Evidence={ECO:0000256|ARBA:ARBA00023544}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586; CC Evidence={ECO:0000256|ARBA:ARBA00023544}; CC -!- CATALYTIC ACTIVITY: CC Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15- CC oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:79072, ChEBI:CHEBI:133411; CC Evidence={ECO:0000256|ARBA:ARBA00023543}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594; CC Evidence={ECO:0000256|ARBA:ARBA00023543}; CC -!- CATALYTIC ACTIVITY: CC Reaction=20-hydroxy-leukotriene B4 + NADP(+) = 12-oxo-20-hydroxy- CC leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:51208, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57460, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:133346; CC Evidence={ECO:0000256|ARBA:ARBA00023517}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51209; CC Evidence={ECO:0000256|ARBA:ARBA00023517}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-hydroxynonanal + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) + CC NADPH; Xref=Rhea:RHEA:64736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:156112; CC Evidence={ECO:0000256|ARBA:ARBA00023553}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64738; CC Evidence={ECO:0000256|ARBA:ARBA00023553}; CC -!- CATALYTIC ACTIVITY: CC Reaction=6-trans-leukotriene B4 + NADP(+) = 12-oxo-(5S)-hydroxy- CC (6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH; CC Xref=Rhea:RHEA:51204, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:90723, ChEBI:CHEBI:133974; CC Evidence={ECO:0000256|ARBA:ARBA00023496}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51205; CC Evidence={ECO:0000256|ARBA:ARBA00023496}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH; CC Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457; CC Evidence={ECO:0000256|ARBA:ARBA00023696}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50618; CC Evidence={ECO:0000256|ARBA:ARBA00023696}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + octanal = (2E)-octenal + H(+) + NADPH; CC Xref=Rhea:RHEA:50780, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748; CC Evidence={ECO:0000256|ARBA:ARBA00023504}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50782; CC Evidence={ECO:0000256|ARBA:ARBA00023504}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + pentan-2-one = (E)-pent-3-en-2-one + H(+) + NADPH; CC Xref=Rhea:RHEA:50788, ChEBI:CHEBI:15378, ChEBI:CHEBI:16472, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145276; CC Evidence={ECO:0000256|ARBA:ARBA00024160}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50790; CC Evidence={ECO:0000256|ARBA:ARBA00024160}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH; CC Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74; CC Evidence={ECO:0000256|ARBA:ARBA00023507}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13739; CC Evidence={ECO:0000256|ARBA:ARBA00023507}; CC -!- CATALYTIC ACTIVITY: CC Reaction=decanal + NADP(+) = (2E)-decenal + H(+) + NADPH; CC Xref=Rhea:RHEA:50612, ChEBI:CHEBI:15378, ChEBI:CHEBI:31457, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133455; CC Evidence={ECO:0000256|ARBA:ARBA00023691}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50614; CC Evidence={ECO:0000256|ARBA:ARBA00023691}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dodecanal + NADP(+) = (2E)-dodecenal + H(+) + NADPH; CC Xref=Rhea:RHEA:50784, ChEBI:CHEBI:15378, ChEBI:CHEBI:27836, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133741; CC Evidence={ECO:0000256|ARBA:ARBA00023530}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50786; CC Evidence={ECO:0000256|ARBA:ARBA00023530}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexanal + NADP(+) = (E)-hex-2-enal + H(+) + NADPH; CC Xref=Rhea:RHEA:50776, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:88528; CC Evidence={ECO:0000256|ARBA:ARBA00034052}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50778; CC Evidence={ECO:0000256|ARBA:ARBA00034052}; CC -!- CATALYTIC ACTIVITY: CC Reaction=leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + H(+) + CC NADPH; Xref=Rhea:RHEA:50608, ChEBI:CHEBI:15378, ChEBI:CHEBI:57461, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133309; CC Evidence={ECO:0000256|ARBA:ARBA00023545}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609; CC Evidence={ECO:0000256|ARBA:ARBA00023545}; CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000256|ARBA:ARBA00011852}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family. CC {ECO:0000256|ARBA:ARBA00010460}. 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:KAF5307610.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JABVZW010000169; KAF5307610.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7J7BP38; -. DR Proteomes; UP000563990; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0036132; F:13-prostaglandin reductase activity; IEA:UniProtKB-EC. DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC. DR CDD; cd08294; leukotriene_B4_DH_like; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR041694; ADH_N_2. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR045010; MDR_fam. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020843; PKS_ER. DR InterPro; IPR014190; PTGR1. DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1. DR PANTHER; PTHR43205:SF7; PROSTAGLANDIN REDUCTASE 1; 1. DR Pfam; PF16884; ADH_N_2; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; GroES-like; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501}; KW Reference proteome {ECO:0000313|Proteomes:UP000563990}. FT DOMAIN 20..331 FT /note="Enoyl reductase (ER)" FT /evidence="ECO:0000259|SMART:SM00829" SQ SEQUENCE 333 AA; 36552 MW; F7E3F12B7B78BFAC CRC64; MTKAKVYLLQ KYFEGLPKEG DLEIVEENLP PLKDGEFLAE ALYWSVDPYM RPAAARLKLG TPFIGHQVAK IIDSKSKEYR EGTIVVGAFG WRTHTISDGR SNVSATPGVW KVPDLGDLPL SLAIGMLGRV GNTAYFGFLE LCQPKQGETV VVSGAGGAVG SHVGQIAKIK GCKVIGITGS DEKGEWLVNE LGFDCFINYK KPNFANTLTE YTPQGVDCYF DNVGGELSST IISRMNKYGR VSVCGSISSY NATTPVLAPI LQPMLVYSEL KMEGFVVHRW ADRWQEGILQ NLKWIQEGKL KYKETVTKGF ENMFSAFVGM LQGDNVGKAV VKV //