ID H3D8L8_TETNG Unreviewed; 329 AA.
AC H3D8L8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000016859.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000016859.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000256|ARBA:ARBA00010460}.
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DR AlphaFoldDB; H3D8L8; -.
DR STRING; 99883.ENSTNIP00000016859; -.
DR Ensembl; ENSTNIT00000017073.1; ENSTNIP00000016859.1; ENSTNIG00000013855.1.
DR GeneTree; ENSGT00940000154810; -.
DR HOGENOM; CLU_026673_29_3_1; -.
DR InParanoid; H3D8L8; -.
DR OMA; PIKNIHN; -.
DR TreeFam; TF324201; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:ARBA00022501};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022501};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303}.
FT DOMAIN 15..327
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 329 AA; 35794 MW; 7A4998DEC84B8551 CRC64;
MVQAKSWILT KHFDGFPNDS NFELKVEELV EPKDGEVLLE AVFLSVDPYM RPFSALRMKE
GDVMIGTQVA KVVQSKNSAF PVGTHVVARC GWRTHTVCDG TPLTPILPKW PEDVSLSLAL
GTIGMPGLTA LFGIEEVLKL QKGETLLVNA AAGAVGTVVG QIAKIKGCKV VGSAGSDAKV
AYLKELGFDE AFNYKTVGSL EEALKKASPD GYDCFFENVG GPFSTVALQQ MKAFGRIAVC
GGIATYNDKT QQTGSYPPLT IIFKQLKMEG FMQSRWEHKH PESLKRLMGW LKEGKLQSRE
HVTKGFENMP AAFMGMLRGE NTGKAIVAV
//
