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Reviewed, UniProtKB/Swiss-Prot Q29073 (PTGR1_PIG)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Prostaglandin reductase 1
      Short name=PRG-1
    EC=1.3.1.-
Alternative name(s):
    NADP-dependent leukotriene B4 12-hydroxydehydrogenase
    EC=1.3.1.74
    15-oxoprostaglandin 13-reductase
    EC=1.3.1.48
Gene names
Name: PTGR1
Synonyms: LTB4DH
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and 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. Ref.2

Catalytic activity

n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H.

11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)+ = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H.

Subunit structure

Monomer or homodimer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Ubiquitously distributed in various tissues and leukocytes, the kidney and liver had the highest enzyme activities.

Sequence similarities

Belongs to the NADP-dependent oxidoreductase L4BD family.

biophysicochemical properties

Kinetic parameters:

KM=7.7 µM for 15-oxo-PGE1

KM=19 µM for 15-oxo-PGE2

KM=10 µM for LTB4

KM=153 µM for NADH

KM=15 µM for NADPH

Vmax=2470 nmol/min/mg enzyme with 15-keto-PGE1 as substrate

Vmax=847 nmol/min/mg enzyme with 15-keto-PGE2 as substrate

Vmax=7.0 nmol/min/mg enzyme with LTB4 as substrate

Vmax=2352 nmol/min/mg enzyme with NADH as substrate

Vmax=729 nmol/min/mg enzyme with NADPH as substrate

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function15-oxoprostaglandin 13-oxidase activity

Inferred from electronic annotation. Source: EC

2-alkenal reductase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Prostaglandin reductase 1
PRO_0000218067

Regions

Nucleotide binding149 – 16618NADP Potential
Compositional bias250 – 2578Pro-rich

Sites

Binding site1781NADP By similarity
Binding site1931NADP By similarity
Binding site2171NADP By similarity
Binding site2451NADP By similarity
Binding site3211NADP By similarity

Experimental info

Mutagenesis1491A → E: Reduces activity by 90%. Ref.1
Mutagenesis1491A → V: Reduces activity by half. Ref.1
Mutagenesis1501A → V: No effect. Ref.1
Mutagenesis1521G → V: Loss of activity. Ref.1
Mutagenesis1551G → V: Reduces activity by 99%. Ref.1
Mutagenesis1591G → V: Reduces activity by 60%. Ref.1
Mutagenesis1661G → V: Reduces activity by 99%. Ref.1
Sequence conflict1181T → A in AAC39170. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q29073-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: D8893061A7EFBEEA

FASTA32935,762
        10         20         30         40         50         60 
MVRAKSWTLK KHFVGYPTPS NFELKTVELP PLKNGEVLLE ALFLTVDPYM RIAARKLKEG 

        70         80         90        100        110        120 
DMMMGEQVAR VIESKNAAFP TGTIVVALLG WTTHSISDGK NLERLLAEWP DTLPLSLTLG 

       130        140        150        160        170        180 
TVGMPGLTAY FGLLDICGLK GGETVMVNAA AGAVGSVVGQ IAKLKGCKVV GAAGSDEKVA 

       190        200        210        220        230        240 
CLKKYGFDVA FNYKTIESLE ETLKKASPEG YDCYFDNVGG EFSNAVTSQM KKFGRIAICG 

       250        260        270        280        290        300 
AISTYNRTGP PPPGPPPEVV IYNELCFQGF IVTRWQGEVR QKALRDLLKW VSEGKIQYHE 

       310        320 
HITEGFENMP AAFMGMLKGE NLGKAIVKA

« Hide

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References

[1]"cDNA cloning, expression, and mutagenesis study of leukotriene B4 12-hydroxydehydrogenase."
Yokomizo T., Ogawa Y., Uozumi N., Kume K., Izumi T., Shimizu T.
J. Biol. Chem. 271:2844-2850(1996) [PubMed: 8576264] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF ALA-149; ALA-150; GLY-152; GLY-155; GLY-159 AND GLY-166.
Tissue: Kidney.
[2]"Purification, cDNA cloning and expression of 15-oxoprostaglandin 13-reductase from pig lung."
Ensor C.M., Zhang H., Tai H.-H.
Biochem. J. 330:103-108(1998) [PubMed: 9461497] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
Tissue: Lung.
[3]"Enzymatic inactivation of leukotriene B4 by a novel enzyme found in the porcine kidney. Purification and properties of leukotriene B4 12-hydroxydehydrogenase."
Yokomizo T., Izumi T., Takahashi T., Kasama T., Kobayashi Y., Sato F., Taketani Y., Shimizu T.
J. Biol. Chem. 268:18128-18135(1993) [PubMed: 8394361] [Abstract]
Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 1-15.
Tissue: Kidney.

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Cross-references

Sequence databases

D49386 mRNA. Translation: BAA08381.1.
U87622 mRNA. Translation: AAC39170.1.
PIRA47421.
RefSeqNP_999550.1.
UniGeneSsc.14490

3D structure databases

SMRQ29073. Positions 1-329.
ModBaseSearch...

Genome annotation databases

GeneID397678.
KEGGssc:397678.

Phylogenomic databases

HOVERGENQ29073.

Enzyme and pathway databases

BRENDA1.3.1.48. 249.
1.3.1.74. 249.

Family and domain databases

InterProIPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR014190. B4_12hDH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR02825. B4_12hDH. 1 hit.
ProtoNetSearch...

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Entry information

Entry namePTGR1_PIG
AccessionPrimary (citable) accession number: Q29073
Secondary accession number(s): O62642
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents