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UniProtKB/Swiss-Prot entry Q9EQZ5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PTGR1_CAVPO
Primary accession number Q9EQZ5
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
Name and origin of the protein
Protein name Prostaglandin reductase 1
Synonyms PRG-1
EC 1.3.1.-
NADP-dependent leukotriene B4 12-hydroxydehydrogenase
LTB4
12-HD
EC 1.3.1.74
15-oxoprostaglandin 13-reductase
PGR
EC 1.3.1.48
Gene name
Name: Ptgr1
Synonyms: Ltb4dh
From
Cavia porcellus (Guinea pig) [TaxID: 10141] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Hystricognathi; Caviidae; Cavia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=11733004 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto T., Yokomizo T., Nakao A., Izumi T., Shimizu T.;
"Immunohistochemical localization of guinea-pig leukotriene B4 12-hydroxydehydrogenase/15-ketoprostaglandin 13-reductase.";
Eur. J. Biochem. 268:6105-6113(2001).
[2]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH NADP AND SUBSTRATE.
DOI=10.1074/jbc.M312655200; PubMed=15007077 [NCBI, ExPASy, EBI, Israel, Japan]
Hori T., Yokomizo T., Ago H., Sugahara M., Ueno G., Yamamoto M., Kumasaka T., Shimizu T., Miyano M.;
"Structural basis of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase catalytic mechanism and a possible Src homology 3 domain binding loop.";
J. Biol. Chem. 279:22615-22623(2004).
Comments
  • FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4.
  • CATALYTIC ACTIVITY: n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H.
  • CATALYTIC ACTIVITY: 11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)+ = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=93 µM for LTB4;
    KM=35 µM for 15-keto-PGE2;
    Vmax=1.7 nmol/min/mg enzyme with LTB4 as substrate;
    Vmax=345 nmol/min/mg enzyme with 15-keto-PGE2 as substrate;
  • SUBUNIT: Monomer or homodimer.
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity).
  • TISSUE SPECIFICITY: Detected in small intestine, kidney, liver, spleen and stomach (at protein level). Detected in small intestine, kidney and liver.
  • SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB021219; BAB20289.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1V3T; X-ray; 2.30 A; A/B=1-329.[ExPASy / RCSB / EBI]
1V3U; X-ray; 2.00 A; A/B=1-329.[ExPASy / RCSB / EBI]
1V3V; X-ray; 2.00 A; A/B=1-329.[ExPASy / RCSB / EBI]
2DM6; X-ray; 2.00 A; A/B=1-329.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1V3T; -.
1V3U; -.
1V3V; -.
2DM6; -.
ModBase Q9EQZ5.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0047522; Molecular function: 15-oxoprostaglandin 13-oxidase activity (inferred from electronic annotation from EC).
GO:0032440; Molecular function: 2-alkenal reductase activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR014190; B4_12hDHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02825; B4_12hDH; 1.
ProtoNet Q9EQZ5.
Phylogenomic databases
HOVERGEN Q9EQZ5; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   329  329     Prostaglandin reductase 1. PRO_0000218064
NP_BIND   149   166  18     NADP (Potential). 
BINDING   178   178        NADP. 
BINDING   193   193        NADP. 
BINDING   217   217        NADP. 
BINDING   245   245        NADP. 
BINDING   321   321        NADP. 
STRAND   3     9  7      
STRAND   14    16  3      
HELIX   19    21  3      
STRAND   22    28  7      
STRAND   37    45  9      
HELIX   49    53  5      
HELIX   54    56  3      
STRAND   67    75  9      
STRAND   84    87  4      
STRAND   91    97  7      
STRAND   99   101  3      
HELIX   115   119  5      
TURN   120   122  3      
HELIX   124   134  11      
TURN   135   137  3      
STRAND   144   149  6      
HELIX   153   164  12      
STRAND   168   175  8      
HELIX   176   184  9      
STRAND   188   192  5      
TURN   193   195  3      
HELIX   199   206  8      
STRAND   211   218  8      
HELIX   220   227  8      
STRAND   230   238  9      
HELIX   242   244  3      
HELIX   257   262  6      
STRAND   266   269  4      
HELIX   272   274  3      
HELIX   277   292  16      
STRAND   300   304  5      
HELIX   306   308  3      
HELIX   309   318  10      
STRAND   322   328  7      
Sequence information
Length: 329 AA [This is the length of the unprocessed precursor] Molecular weight: 35730 Da [This is the MW of the unprocessed precursor] CRC64: 8C5D86D9D2C9FEA1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVKAKSWTLK KHFQGKPTQS DFELKTVELP PLKNGEVLLE ALFLSVDPYM RIASKRLKEG 

        70         80         90        100        110        120 
AVMMGQQVAR VVESKNSAFP AGSIVLAQSG WTTHFISDGK GLEKLLTEWP DKLPLSLALG 

       130        140        150        160        170        180 
TIGMPGLTAY FGLLEVCGVK GGETVLVSAA AGAVGSVVGQ IAKLKGCKVV GAAGSDEKIA 

       190        200        210        220        230        240 
YLKQIGFDAA FNYKTVNSLE EALKKASPDG YDCYFDNVGG EFLNTVLSQM KDFGKIAICG 

       250        260        270        280        290        300 
AISVYNRMDQ LPPGPSPESI IYKQLRIEGF IVYRWQGDVR EKALRDLMKW VLEGKIQYHE 

       310        320 
HVTKGFENMP AAFIEMLNGA NLGKAVVTA
Q9EQZ5 in FASTA format

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