ID A0A158NP60_ATTCE Unreviewed; 510 AA. AC A0A158NP60; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 24-JAN-2024, entry version 29. 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}; GN Name=105622509 {ECO:0000313|EnsemblMetazoa:XP_012059318.1}; OS Atta cephalotes (Leafcutter ant). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea; OC Formicidae; Myrmicinae; Atta. OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012059318.1, ECO:0000313|Proteomes:UP000005205}; RN [1] {ECO:0000313|Proteomes:UP000005205} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007; RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E., RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E., RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E., RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E., RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S., RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S., RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F., RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D., RA Weinstock G.M., Gerardo N.M., Currie C.R.; RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals RT insights into its obligate symbiotic lifestyle."; RL PLoS Genet. 7:e1002007-e1002007(2011). RN [2] {ECO:0000313|EnsemblMetazoa:XP_012059318.1} RP IDENTIFICATION. RG EnsemblMetazoa; RL Submitted (APR-2016) to UniProtKB. 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}. 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; ADTU01001531; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_012059318.1; XM_012203928.1. DR AlphaFoldDB; A0A158NP60; -. DR STRING; 12957.A0A158NP60; -. DR EnsemblMetazoa; XM_012203928.1; XP_012059318.1; LOC105622509. DR GeneID; 105622509; -. DR KEGG; acep:105622509; -. DR eggNOG; KOG4169; Eukaryota. DR InParanoid; A0A158NP60; -. DR OrthoDB; 2082185at2759; -. DR Proteomes; UP000005205; Unassembled WGS sequence. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. 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; 2. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000005205}. SQ SEQUENCE 510 AA; 54956 MW; D5A5DA5E437A84BD CRC64; MEAKGRVALI TGAASGIGKA YATELLNQGA KVAICDINTE EGEKLVETLS EKYGKGRVIF SQCDVTDYLQ FEESFQTTIT EFGHIDIVIN NAGIMNDRFW ELEVDINLNG VIRGTLLAQR FMGTDRGGQG GVVINTGSNV SINPYVSVPI YSATKAALVS FTRAFGDQYH VDLTGVKVMA LCPGTTDTKL VRDVNRKLLL ARYEDAWQKD IVSSIPQRAE HVAKALIHVL STGKSGSVWM VEKDQPPHEI RKTVLITGGA NGIGYCTARE LLRSGVKAIA IIDLPDSNGE NAVTELEKEF GANHAIFLTG DVANIEELTA CFKKAIESFG TLDIVINNAG IMNDADWEPM VDVNYKGVVR GTILGLNHMG KHKGGKGGTI VNMSSIIGLQ GNPIAPIYAG TSFAIIGFTS SLLTFYEKTG VRVLLICPGL TTTGLASKFM SSKIYAMDLL DDEIAAKEMT TMESQSPEHV ATAIVELIEK GGNGTVFVSE NNQPTYAVQL PIYTDLKISI //