ID A0A023FB52_TRIIF Unreviewed; 261 AA. AC A0A023FB52; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 24-JUL-2024, entry version 23. DE RecName: Full=15-hydroxyprostaglandin dehydrogenase [NAD(+)] {ECO:0000256|ARBA:ARBA00040276}; DE EC=1.1.1.141 {ECO:0000256|ARBA:ARBA00038968}; DE EC=1.1.1.232 {ECO:0000256|ARBA:ARBA00039060}; DE AltName: Full=Eicosanoid/docosanoid dehydrogenase [NAD(+)] {ECO:0000256|ARBA:ARBA00042026}; DE AltName: Full=Prostaglandin dehydrogenase 1 {ECO:0000256|ARBA:ARBA00041812}; OS Triatoma infestans (Assassin bug). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera; OC Cimicomorpha; Reduviidae; Triatominae; Triatoma. OX NCBI_TaxID=30076 {ECO:0000313|EMBL:JAC18707.1}; RN [1] {ECO:0000313|EMBL:JAC18707.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Chile {ECO:0000313|EMBL:JAC18707.1}; RC TISSUE=Salivary glands {ECO:0000313|EMBL:JAC18707.1}; RX PubMed=25474469; RA Schwarz A., Medrano-Mercado N., Schaub G.A., Struchiner C.J., Bargues M.D., RA Levy M.Z., Ribeiro J.M.; RT "An updated insight into the Sialotranscriptome of Triatoma infestans: RT developmental stage and geographic variations."; RL PLoS Negl. Trop. Dis. 8:E3372-E3372(2014). CC -!- CATALYTIC ACTIVITY: CC Reaction=(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + NAD(+) = 11- CC oxo-(5Z,8Z,12E,14Z)-eicosatetraenoate + H(+) + NADH; CC Xref=Rhea:RHEA:48640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78836, ChEBI:CHEBI:90697; CC Evidence={ECO:0000256|ARBA:ARBA00036144}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48641; CC Evidence={ECO:0000256|ARBA:ARBA00036144}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + NAD(+) = 15- CC oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + NADH; CC Xref=Rhea:RHEA:23260, ChEBI:CHEBI:15378, ChEBI:CHEBI:57409, CC ChEBI:CHEBI:57410, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=1.1.1.232; Evidence={ECO:0000256|ARBA:ARBA00035872}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23261; CC Evidence={ECO:0000256|ARBA:ARBA00035872}; CC -!- CATALYTIC ACTIVITY: CC Reaction=14-hydroxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate + NAD(+) = CC 14-oxo-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate + H(+) + NADH; CC Xref=Rhea:RHEA:48952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:90866, ChEBI:CHEBI:90867; CC Evidence={ECO:0000256|ARBA:ARBA00036093}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48953; CC Evidence={ECO:0000256|ARBA:ARBA00036093}; CC -!- CATALYTIC ACTIVITY: CC Reaction=15-oxo-(5S,6R)-dihydroxy-(7E,9E,11Z)-eicosatrienoate + H(+) + CC NADH = (5S,6R,15S)-trihydroxy-(7E,9E,11Z)-eicosatrienoate + NAD(+); CC Xref=Rhea:RHEA:41596, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:78325, ChEBI:CHEBI:78329; CC Evidence={ECO:0000256|ARBA:ARBA00036136}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41597; CC Evidence={ECO:0000256|ARBA:ARBA00036136}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + prostaglandin A1 = 15-oxo-prostaglandin A1 + H(+) + CC NADH; Xref=Rhea:RHEA:41263, ChEBI:CHEBI:15378, ChEBI:CHEBI:57398, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:85072; CC Evidence={ECO:0000256|ARBA:ARBA00036411}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41264; CC Evidence={ECO:0000256|ARBA:ARBA00036411}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + prostaglandin E1 = 15-oxoprostaglandin E1 + H(+) + CC NADH; Xref=Rhea:RHEA:16477, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397, CC ChEBI:CHEBI:57401, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC Evidence={ECO:0000256|ARBA:ARBA00036041}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16478; CC Evidence={ECO:0000256|ARBA:ARBA00036041}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) + CC NADH; Xref=Rhea:RHEA:11876, ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:606564; CC EC=1.1.1.141; Evidence={ECO:0000256|ARBA:ARBA00036860}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11877; CC Evidence={ECO:0000256|ARBA:ARBA00036860}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + resolvin D1 = 17-oxoresolvin D1 + H(+) + NADH; CC Xref=Rhea:RHEA:50128, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132081; CC Evidence={ECO:0000256|ARBA:ARBA00036236}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50129; CC Evidence={ECO:0000256|ARBA:ARBA00036236}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + resolvin D1 = 8-oxoresolvin D1 + H(+) + NADH; CC Xref=Rhea:RHEA:50124, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132080; CC Evidence={ECO:0000256|ARBA:ARBA00036621}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50125; CC Evidence={ECO:0000256|ARBA:ARBA00036621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + resolvin D2 = 16-oxoresolvin D2 + H(+) + NADH; CC Xref=Rhea:RHEA:53588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137498; CC Evidence={ECO:0000256|ARBA:ARBA00036962}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53589; CC Evidence={ECO:0000256|ARBA:ARBA00036962}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + resolvin D2 = 7-oxoresolvin D2 + H(+) + NADH; CC Xref=Rhea:RHEA:53584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137497; CC Evidence={ECO:0000256|ARBA:ARBA00036456}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53585; CC Evidence={ECO:0000256|ARBA:ARBA00036456}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + resolvin E1 = 18-oxo-resolvin E1 + H(+) + NADH; CC Xref=Rhea:RHEA:49244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:91000, ChEBI:CHEBI:91001; CC Evidence={ECO:0000256|ARBA:ARBA00036728}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49245; CC Evidence={ECO:0000256|ARBA:ARBA00036728}; CC -!- CATALYTIC ACTIVITY: CC Reaction=lipoxin A4 + NAD(+) = 15-oxo-(5S,6R)-dihydroxy- CC (7E,9E,11Z,13E)-eicosatetraenoate + H(+) + NADH; CC Xref=Rhea:RHEA:41572, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:67026, ChEBI:CHEBI:78311; CC Evidence={ECO:0000256|ARBA:ARBA00036528}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41573; CC Evidence={ECO:0000256|ARBA:ARBA00036528}; CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}. 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; GBBI01000005; JAC18707.1; -; mRNA. DR AlphaFoldDB; A0A023FB52; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0016404; F:15-hydroxyprostaglandin dehydrogenase (NAD+) activity; IEA:TreeGrafter. DR GO; GO:0007565; P:female pregnancy; IEA:TreeGrafter. DR GO; GO:0006693; P:prostaglandin metabolic process; IEA:TreeGrafter. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020904; Sc_DH/Rdtase_CS. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR44229; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1. DR PANTHER; PTHR44229:SF4; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 2: Evidence at transcript level; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. SQ SEQUENCE 261 AA; 28602 MW; 460651C8C05311B2 CRC64; MELKGAVALV TGAAQGIGKA CVDYLLAEGV KVMITDISKT VGEATEKEMA TKHGESNVEF IYCDVTNDEC FEDSFKETIK KFDKLDLLIN NAGIANELMD DGWKQTIQIN FIAVVKGTYL GMKYMGKHEG KPGGTIVNIG SMSSFVPFES TPVYSATKAA VNQFSRSIST KLHYDRTGVR VISVNPAFTD TAILPAITKQ IDKSTKTSFL NAWKEHKVQS VDNMGKGMIT VLKKAEPGSL WVIQDDVAPK RIELKVIKHD N //