Reviewed, UniProtKB/Swiss-Prot Q9EQZ5 (PTGR1_CAVPO)

Names and origin

Protein names

Recommended name:
    Prostaglandin reductase 1
      Short name=PRG-1
    EC=1.3.1.-
Alternative name(s):
    NADP-dependent leukotriene B4 12-hydroxydehydrogenase
      Short name=LTB4
      Short name=12-HD
    EC=1.3.1.74
    15-oxoprostaglandin 13-reductase
      Short name=PGR
    EC=1.3.1.48

Gene names

Name:	Ptgr1
Synonyms:	Ltb4dh

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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. 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.1
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.
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. Ref.1
Sequence similarities	Belongs to the NADP-dependent oxidoreductase L4BD family.
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

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	15-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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 329

329

Prostaglandin reductase 1

PRO_0000218064

Regions

Nucleotide binding

149 – 166

18

NADP Potential

Sites

Binding site

178

1

NADP

Binding site

193

1

NADP

Binding site

217

1

NADP

Binding site

245

1

NADP

Binding site

321

1

NADP

Secondary structure

1

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329

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Beta strand

14 – 16

3

Helix

19 – 21

3

Beta strand

22 – 28

7

Beta strand

37 – 45

9

Helix

49 – 53

5

Helix

54 – 56

3

Beta strand

67 – 75

9

Beta strand

84 – 87

4

Beta strand

91 – 97

7

Beta strand

99 – 101

3

Helix

115 – 119

5

Turn

120 – 122

3

Helix

124 – 134

11

Turn

135 – 137

3

Beta strand

144 – 149

6

Helix

153 – 164

12

Beta strand

168 – 175

8

Helix

176 – 184

9

Beta strand

188 – 192

5

Turn

193 – 195

3

Helix

199 – 206

8

Beta strand

211 – 218

8

Helix

220 – 227

8

Beta strand

230 – 238

9

Helix

242 – 244

3

Helix

257 – 262

6

Beta strand

266 – 269

4

Helix

272 – 274

3

Helix

277 – 292

16

Beta strand

300 – 304

5

Helix

306 – 308

3

Helix

309 – 318

10

Beta strand

322 – 328

7

Sequences

	Sequence		Length	Mass (Da)
	Q9EQZ5-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 8C5D86D9D2C9FEA1	FASTA	329	35,730
	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

References

[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: 11733004] [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: 15007077] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH NADP AND SUBSTRATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB021219 mRNA. Translation: BAB20289.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V3T	X-ray	2.30	A/B	1-329	[»]
1V3U	X-ray	2.00	A/B	1-329	[»]
1V3V	X-ray	2.00	A/B	1-329	[»]
2DM6	X-ray	2.00	A/B	1-329	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

Q9EQZ5.

Enzyme and pathway databases

BRENDA

1.3.1.48. 44.
1.3.1.74. 44.

Family and domain databases

InterPro

IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR014190. B4_12hDH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF00107. ADH_zinc_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02825. B4_12hDH. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PTGR1_CAVPO

Accession

Primary (citable) accession number: Q9EQZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	March 1, 2001
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)