UniProt: B5X7T0

Database: UniProt
Entry: B5X7T0_SALSA

LinkDB:  B5X7T0_SALSA 
Original site:  B5X7T0_SALSA

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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ID   B5X7T0_SALSA            Unreviewed;       348 AA.
AC   B5X7T0;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Prostaglandin reductase 2 {ECO:0000256|ARBA:ARBA00020652};
DE            EC=1.3.1.48 {ECO:0000256|ARBA:ARBA00011981};
DE   AltName: Full=15-oxoprostaglandin 13-reductase {ECO:0000256|ARBA:ARBA00033119};
GN   Name=ZADH1 {ECO:0000313|EMBL:ACI66900.1};
GN   Synonyms=zadh1 {ECO:0000313|RefSeq:NP_001134279.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI66900.1};
RN   [1] {ECO:0000313|EMBL:ACI66900.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spleen {ECO:0000313|EMBL:ACI66900.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RA   Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA   Koop B.F.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI66900.1, ECO:0000313|RefSeq:NP_001134279.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spleen {ECO:0000313|EMBL:ACI66900.1};
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
RN   [3] {ECO:0000313|EMBL:ACI66900.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Spleen {ECO:0000313|EMBL:ACI66900.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:NP_001134279.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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 E2 + NAD(+) = 15-
CC         oxoprostaglandin E2 + H(+) + NADH; Xref=Rhea:RHEA:11916,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00023690};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11918;
CC         Evidence={ECO:0000256|ARBA:ARBA00023690};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NADP(+) = 15-
CC         oxoprostaglandin E2 + H(+) + NADPH; Xref=Rhea:RHEA:11912,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00023711};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11914;
CC         Evidence={ECO:0000256|ARBA:ARBA00023711};
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   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC       {ECO:0000256|ARBA:ARBA00010460}.
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DR   EMBL; BT047099; ACI66900.1; -; mRNA.
DR   RefSeq; NP_001134279.1; NM_001140807.1.
DR   STRING; 8030.ENSSSAP00000106260; -.
DR   PaxDb; 8030-ENSSSAP00000106260; -.
DR   GeneID; 100195778; -.
DR   KEGG; sasa:100195778; -.
DR   CTD; 145482; -.
DR   OrthoDB; 179761at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa01.
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   CDD; cd08293; PTGR2; 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; IPR037399; PTGR2.
DR   PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR   PANTHER; PTHR43205:SF5; PROSTAGLANDIN REDUCTASE 2; 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; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          14..344
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   348 AA;  37762 MW;  6A496A2D62C04C57 CRC64;
     MLLVQRVVLN SRPGTDEEPV PGHFRVEEAI VGPFLKEGQV LVRTLFLSVD PYMRCRMNDD
     TGAEYLAPWG LSECVDGGGV GVVELSRCES LSVDDMVTSF NWHWQTQCLM DEKLLQKVEP
     QLVDGHISYF LGAVGMPGLT ALLGVREKGH VTEGANQTMV VSGAAGACGS IAGQIGRVDG
     CTRVVGICGS DEKCRVLVED LGFSAAVNYR QGDVATALKE SCPDGVDVYF DNVGGPISDA
     VIAQMNNDGH VILCGQISQY NKDVPYPPPL CDETQEALQS KNITRERFMV LNYMEKHEAG
     IIQLSQWVRE GQIKVLETVV DGIENMGVAF CSMMKGGNIG KQIIKISD
//

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