Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O73888 (HPGDS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hematopoietic prostaglandin D synthase

Short name=H-PGDS
EC=5.3.99.2
Alternative name(s):
GST class-sigma
Glutathione S-transferase
EC=2.5.1.18
Glutathione-dependent PGD synthase
Glutathione-requiring prostaglandin D synthase
Prostaglandin-H2 D-isomerase
Gene names
Name:HPGDS
Synonyms:GSTS, PGDS, PTGDS2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides, organic isothiocyanates and alpha,beta-unsaturated carbonyls. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide and t-butyl hydroperoxide. Ref.1

Catalytic activity

(5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate. Ref.1

RX + glutathione = HX + R-S-glutathione. Ref.1

Cofactor

Glutathione. Required for the prostaglandin D synthase activity. Ref.1

Subcellular location

Cytoplasm.

Tissue specificity

Highly expressed in liver, kidney, small intestine and colon, moderately in pancreas, bone marrow, lung and ovary, and expressed at low levels in spleen, thymus, heart and brain. Not detected in oviduct or skin (at protein level). Ref.1

Sequence similarities

Belongs to the GST superfamily. Sigma family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

Vmax=128 µmol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate Ref.1

Vmax=97 µmol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate

Vmax=410 µmol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate

Vmax=116 µmol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate

Vmax=67 µmol/min/mg enzyme with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole as substrate

Vmax=1.4 µmol/min/mg enzyme with 4-nitrobenzyl chloride as substrate

Vmax=0.05 µmol/min/mg enzyme with 1,2-dichloro-4-nitrobenzene as substrate

Vmax=0.04 µmol/min/mg enzyme with ethacrynic acid as substrate

Vmax=2.8 µmol/min/mg enzyme with 4-hydroxynon-2-enal as substrate

Vmax=0.06 µmol/min/mg enzyme with trans,trans-deca-2,4-dienal as substrate

Vmax=0.02 µmol/min/mg enzyme with trans-non-2-enal as substrate

Vmax=0.5 µmol/min/mg enzyme with cumene hydroperoxide as substrate

Vmax=0.06 µmol/min/mg enzyme with t-butyl hydroperoxide as substrate

Vmax=12.6 µmol/min/mg enzyme with allyl isothiocyanate as substrate

Vmax=17.6 µmol/min/mg enzyme with benzyl isothiocyanate as substrate

Vmax=0.02 µmol/min/mg enzyme with Delta5-androstene-3,17-dione as substrate

Vmax=0.11 µmol/min/mg enzyme with 4-nitrophenyl acetate as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 199198Hematopoietic prostaglandin D synthase
PRO_0000185937

Regions

Domain2 – 7978GST N-terminal
Domain81 – 199119GST C-terminal
Region63 – 642Glutathione binding By similarity

Sites

Binding site81Glutathione By similarity
Binding site141Glutathione By similarity
Binding site391Glutathione By similarity

Sequences

Sequence LengthMass (Da)Tools
O73888 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 335A884D93009069

FASTA19922,730
        10         20         30         40         50         60 
MPNYKLTYFN LRGRAEICRY LFAYAGIKYE DHRLEGADWP KIKPTIPFGK VPILEVDGVI 

        70         80         90        100        110        120 
IHQSLAIARY LARESGLAGQ TPVEQALADA IVDTIDDFMM LFPWAEKNQD VKEKAFNDIL 

       130        140        150        160        170        180 
TNKAPELLKD LDTFLGDKKW FVGKSVTWAD FYWDVCSTTL LSYKADLADK YPRLLALRDR 

       190 
VEALPAIAAW IQKRPKTAI 

« Hide

References

[1]"Sequence, catalytic properties and expression of chicken glutathione-dependent prostaglandin D2 synthase, a novel class Sigma glutathione S-transferase."
Thomson A.M., Meyer D.J., Hayes J.D.
Biochem. J. 333:317-325(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006405 mRNA. Translation: CAA07005.1.
RefSeqNP_990342.1. NM_205011.1.
UniGeneGga.3137.

3D structure databases

ProteinModelPortalO73888.
SMRO73888. Positions 1-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000016919.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395863.
KEGGgga:395863.

Organism-specific databases

CTD27306.

Phylogenomic databases

HOGENOMHOG000115733.
HOVERGENHBG105321.
InParanoidO73888.
KOK01830.
OMAWDVCSTT.
OrthoDBEOG78WKT1.
PhylomeDBO73888.
TreeFamTF105321.

Enzyme and pathway databases

BRENDA5.3.99.2. 1306.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20815930.
PROO73888.

Entry information

Entry nameHPGDS_CHICK
AccessionPrimary (citable) accession number: O73888
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families