[1]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS OF ALA-149; ALA-150; GLY-152; GLY-155; GLY-159 AND GLY-166. TISSUE=Kidney; DOI=10.1074/jbc.271.5.2844; PubMed=8576264 [NCBI, ExPASy, EBI, Israel, Japan] Yokomizo T., Ogawa Y., Uozumi N., Kume K., Izumi T., Shimizu T.; "cDNA cloning, expression, and mutagenesis study of leukotriene B4 12-hydroxydehydrogenase."; J. Biol. Chem. 271:2844-2850(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION. TISSUE=Lung; PubMed=9461497 [NCBI, ExPASy, EBI, Israel, Japan] Ensor C.M., Zhang H., Tai H.-H.; "Purification, cDNA cloning and expression of 15-oxoprostaglandin 13-reductase from pig lung."; Biochem. J. 330:103-108(1998).
[3]	CHARACTERIZATION, AND PROTEIN SEQUENCE OF 1-15. TISSUE=Kidney; PubMed=8394361 [NCBI, ExPASy, EBI, Israel, Japan] Yokomizo T., Izumi T., Takahashi T., Kasama T., Kobayashi Y., Sato F., Taketani Y., Shimizu T.; "Enzymatic inactivation of leukotriene B4 by a novel enzyme found in the porcine kidney. Purification and properties of leukotriene B4 12-hydroxydehydrogenase."; J. Biol. Chem. 268:18128-18135(1993).

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.
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:	K_M=7.7 µM for 15-oxo-PGE1;
	K_M=19 µM for 15-oxo-PGE2;
	K_M=10 µM for LTB4;
	K_M=153 µM for NADH;
	K_M=15 µM for NADPH;
	V_max=2470 nmol/min/mg enzyme with 15-keto-PGE1 as substrate;
	V_max=847 nmol/min/mg enzyme with 15-keto-PGE2 as substrate;
	V_max=7.0 nmol/min/mg enzyme with LTB4 as substrate;
	V_max=2352 nmol/min/mg enzyme with NADH as substrate;
	V_max=729 nmol/min/mg enzyme with NADPH as substrate;

SUBUNIT: 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.
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

D49386; BAA08381.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U87622; AAC39170.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A47421; A47421.

NP_999550.1; -.

3D structure databases

SMR

Q29073; 1-329.

ModBase

Q29073.

Ontologies

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).
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.

BLOCKS

Q29073.

Genome annotation databases

GeneID

397678; -.

KEGG

ssc:397678; -.

Phylogenomic databases

HOVERGEN

Q29073; -.

Other

ProtoNet

Q29073.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 329`	`329`	`Prostaglandin reductase 1.`	`PRO_0000218067`
`NP_BIND`	`149 166`	`18`	`NADP (Potential).`
`COMPBIAS`	`250 257`	`8`	`Pro-rich.`
`BINDING`	`178 178`		`NADP (By similarity).`
`BINDING`	`193 193`		`NADP (By similarity).`
`BINDING`	`217 217`		`NADP (By similarity).`
`BINDING`	`245 245`		`NADP (By similarity).`
`BINDING`	`321 321`		`NADP (By similarity).`
`MUTAGEN`	`149 149`		`A->E: Reduces activity by 90%.`
`MUTAGEN`	`149 149`		`A->V: Reduces activity by half.`
`MUTAGEN`	`150 150`		`A->V: No effect.`
`MUTAGEN`	`152 152`		`G->V: Loss of activity.`
`MUTAGEN`	`155 155`		`G->V: Reduces activity by 99%.`
`MUTAGEN`	`159 159`		`G->V: Reduces activity by 60%.`
`MUTAGEN`	`166 166`		`G->V: Reduces activity by 99%.`
`CONFLICT`	`118 118`		`T -> A (in Ref. 2; AAC39170).`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 35762 Da [This is the MW of the unprocessed precursor]

CRC64: D8893061A7EFBEEA [This is a checksum on the sequence]

        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

Q29073 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools