GenomeNet

Database: UniProt
Entry: V8NXV2_OPHHA
LinkDB: V8NXV2_OPHHA
Original site: V8NXV2_OPHHA 
ID   V8NXV2_OPHHA            Unreviewed;       329 AA.
AC   V8NXV2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
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   Name=Ptgr1 {ECO:0000313|EMBL:ETE67089.1};
GN   ORFNames=L345_07120 {ECO:0000313|EMBL:ETE67089.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE67089.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE67089.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE67089.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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}.
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:ETE67089.1}.
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; AZIM01001392; ETE67089.1; -; Genomic_DNA.
DR   AlphaFoldDB; V8NXV2; -.
DR   Proteomes; UP000018936; 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:ARBA00022501};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT   DOMAIN          18..327
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   329 AA;  36422 MW;  CBE4CB46750852E0 CRC64;
     MLRAKAWILK KHFEGPPKQS NFELIEINLP NLKDGEMLLE SVFLSVDPYM RPYSKRNMKE
     GDIMIGSQVA RILESRNPSF LVGTFVVATA GWTTHFISNG KDLSPLPPNW PENLPKSLAL
     GTIGMPGLTA YFGLLQICRP KPGDTVLVNS AAGAVGSVVG QIAKIMGCKV VGTAGSDKKL
     DYLKELGFDK VFNYKTVKSL EQALRDASPD GYNCYFDNVG GEFSSVVLEQ MKTYGRIAVC
     GAVSLYNDTQ LKKGPFVQIP MIMKQLYMEG FLVTRWKDRK DEALKAILKW VQEGKIKSRE
     DITKGFQNMP AAFMGMLQGD NFGKAIVEV
//
DBGET integrated database retrieval system