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Protein

Prostaglandin reductase 1

Gene

Ptgr1

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 B4.1 Publication

Catalytic activityi

A n-alkanal + NAD(P)+ = an 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.

Kineticsi

  1. KM=93 µM for LTB4
  2. KM=35 µM for 15-keto-PGE2
  1. Vmax=1.7 nmol/min/mg enzyme with LTB4 as substrate
  2. Vmax=345 nmol/min/mg enzyme with 15-keto-PGE2 as substrate

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei178 – 1781NADP1 Publication
Binding sitei193 – 1931NADP1 Publication
Binding sitei217 – 2171NADP1 Publication
Binding sitei321 – 3211NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 1554NADP1 Publication
Nucleotide bindingi239 – 2457NADP1 Publication
Nucleotide bindingi270 – 2723NADP1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin reductase 1 (EC:1.3.1.-)
Short name:
PRG-1
Alternative name(s):
15-oxoprostaglandin 13-reductase (EC:1.3.1.48)
Short name:
PGR
NADP-dependent leukotriene B4 12-hydroxydehydrogenase (EC:1.3.1.74)
Short name:
12-HD
Short name:
LTB4
Gene namesi
Name:Ptgr1
Synonyms:Ltb4dh
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Prostaglandin reductase 1PRO_0000218064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphothreonineBy similarity
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei178 – 1781N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Expressioni

Tissue specificityi

Detected in small intestine, kidney, liver, spleen and stomach (at protein level). Detected in small intestine, kidney and liver.1 Publication

Interactioni

Subunit structurei

Monomer or homodimer.1 Publication

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Beta strandi14 – 163Combined sources
Helixi19 – 213Combined sources
Beta strandi22 – 287Combined sources
Beta strandi37 – 459Combined sources
Helixi49 – 535Combined sources
Turni54 – 563Combined sources
Beta strandi67 – 759Combined sources
Beta strandi84 – 874Combined sources
Beta strandi91 – 999Combined sources
Beta strandi102 – 1043Combined sources
Helixi115 – 1195Combined sources
Turni120 – 1223Combined sources
Helixi124 – 13411Combined sources
Turni135 – 1373Combined sources
Beta strandi144 – 1496Combined sources
Helixi153 – 16412Combined sources
Beta strandi168 – 1758Combined sources
Helixi176 – 1849Combined sources
Beta strandi188 – 1925Combined sources
Turni193 – 1953Combined sources
Helixi199 – 2068Combined sources
Beta strandi211 – 2188Combined sources
Helixi220 – 2278Combined sources
Beta strandi230 – 2389Combined sources
Turni244 – 2463Combined sources
Helixi257 – 2626Combined sources
Beta strandi266 – 2694Combined sources
Helixi272 – 2743Combined sources
Helixi278 – 29215Combined sources
Beta strandi300 – 3045Combined sources
Helixi306 – 3083Combined sources
Helixi309 – 3179Combined sources
Beta strandi322 – 3287Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V3TX-ray2.30A/B1-329[»]
1V3UX-ray2.00A/B1-329[»]
1V3VX-ray2.00A/B1-329[»]
2DM6X-ray2.00A/B1-329[»]
ProteinModelPortaliQ9EQZ5.
SMRiQ9EQZ5. Positions 1-329.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9EQZ5.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG055024.
InParanoidiQ9EQZ5.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR014190. B4_12hDH.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02825. B4_12hDH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9EQZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKAKSWTLK KHFQGKPTQS DFELKTVELP PLKNGEVLLE ALFLSVDPYM
60 70 80 90 100
RIASKRLKEG AVMMGQQVAR VVESKNSAFP AGSIVLAQSG WTTHFISDGK
110 120 130 140 150
GLEKLLTEWP DKLPLSLALG TIGMPGLTAY FGLLEVCGVK GGETVLVSAA
160 170 180 190 200
AGAVGSVVGQ IAKLKGCKVV GAAGSDEKIA YLKQIGFDAA FNYKTVNSLE
210 220 230 240 250
EALKKASPDG YDCYFDNVGG EFLNTVLSQM KDFGKIAICG AISVYNRMDQ
260 270 280 290 300
LPPGPSPESI IYKQLRIEGF IVYRWQGDVR EKALRDLMKW VLEGKIQYHE
310 320
HVTKGFENMP AAFIEMLNGA NLGKAVVTA
Length:329
Mass (Da):35,730
Last modified:March 1, 2001 - v1
Checksum:i8C5D86D9D2C9FEA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021219 mRNA. Translation: BAB20289.1.
RefSeqiNP_001166451.1. NM_001172980.1.

Genome annotation databases

GeneIDi100135572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021219 mRNA. Translation: BAB20289.1.
RefSeqiNP_001166451.1. NM_001172980.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V3TX-ray2.30A/B1-329[»]
1V3UX-ray2.00A/B1-329[»]
1V3VX-ray2.00A/B1-329[»]
2DM6X-ray2.00A/B1-329[»]
ProteinModelPortaliQ9EQZ5.
SMRiQ9EQZ5. Positions 1-329.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100135572.

Organism-specific databases

CTDi22949.

Phylogenomic databases

HOVERGENiHBG055024.
InParanoidiQ9EQZ5.

Miscellaneous databases

EvolutionaryTraceiQ9EQZ5.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR014190. B4_12hDH.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02825. B4_12hDH. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Immunohistochemical localization of guinea-pig leukotriene B4 12-hydroxydehydrogenase/15-ketoprostaglandin 13-reductase."
    Yamamoto T., Yokomizo T., Nakao A., Izumi T., Shimizu T.
    Eur. J. Biochem. 268:6105-6113(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Structural basis of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase catalytic mechanism and a possible Src homology 3 domain binding loop."
    Hori T., Yokomizo T., Ago H., Sugahara M., Ueno G., Yamamoto M., Kumasaka T., Shimizu T., Miyano M.
    J. Biol. Chem. 279:22615-22623(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH NADP AND SUBSTRATE.

Entry informationi

Entry nameiPTGR1_CAVPO
AccessioniPrimary (citable) accession number: Q9EQZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.