3-beta-hydroxy-Delta(5)-steroid dehydrogenase
     (EC 1.1.1.145)
     (3-beta-hydroxy-5-ene steroid dehydrogenase)
     (Progesterone reductase)
Steroid Delta-isomerase
     (EC 5.3.3.1)
     (Delta-5-3-ketosteroid isomerase)

Gene name

	Name:	HSD3B
	Synonyms:	3b-HSD

From

Sus scrofa (Pig)

[TaxID: 9823]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.

Protein existence

2: Evidence at transcript level;

References

[1]

NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adipose tissue;
DOI=10.1046/j.1365-2052.2001.00775.x; PubMed=11683717 [NCBI, ExPASy, EBI, Israel, Japan]
von Teichman A., Joerg H., Werner P., Brenig B., Stranzinger G.;
"cDNA cloning and physical mapping of porcine 3 beta-hydroxysteroid dehydrogenase/Delta 5-delta 4 isomerase.";
Anim. Genet. 32:298-302(2001).

Comments

FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.
CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta⁵-steroid + NAD⁺ = a 3-oxo-Delta⁵-steroid + NADH.
CATALYTIC ACTIVITY: A 3-oxo-Delta⁵-steroid = a 3-oxo-Delta⁴-steroid.
PATHWAY: Lipid metabolism; steroid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
SIMILARITY: Belongs to the 3-beta-HSD 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

AF232699; AAF37295.2; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001004049.1; -.

UniGene

Ssc.14393

3D structure databases

ModBase

Q9N119.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003854;	Molecular function: 3-beta-hydroxy-delta5-steroid dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004769;	Molecular function: steroid delta-isomerase activity (inferred from electronic annotation from EC).
GO:0006700;	Biological process: C21-steroid hormone biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002225; 3Beta_OHSteriod_DHase/Estase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

Pfam

PF01073; 3Beta_HSD; 1.
Pfam graphical view of domain structure.

ProtoNet

Q9N119.

Genome annotation databases

GeneID

445539; -.

KEGG

ssc:445539; -.

Phylogenomic databases

HOVERGEN

Q9N119; -.

Other

UniRef

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

Keywords

Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 373`	`372`	`3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase.`	`PRO_0000087786`
`TRANSMEM`	`292 309`	`18`	`Potential.`

Sequence information

Length: 373 AA [This is the length of the unprocessed precursor]

Molecular weight: 41882 Da [This is the MW of the unprocessed precursor]

CRC64: 8BD4FEEF0117F6FF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGWSCLVTG GGGFLGQRIV HLLLEEKDLQ EIRVLDKVFK PEVREEFSKL QSKIKLTMLE 

        70         80         90        100        110        120 
GDILDEQCLK GACQGASVVI HTASIIDVVN AVGRETVMKV NVKGTQLLLE ACVQASVPVF 

       130        140        150        160        170        180 
IHTSSIEVAG PNSYREVIQN ACEEDRLETA WSAPYPLSKK LAEKAVLEAN GWALQNGGTL 

       190        200        210        220        230        240 
HTCALRPMYI YGEGSPFIFA HMNKALENNG VLTHNSKFSR VNPVYVGNVA WAHILALRAL 

       250        260        270        280        290        300 
RDPRKALSVQ GQFYYVADDT PPQSYDDLNY TLGKEWGFCL DSRRSLPPSL RYWLAFLLEI 

       310        320        330        340        350        360 
VSFLLSPIYN YQPPFNRHFV TLCNSVFTVS YKKAQRDLGY EPLFTWEEAK QKTKAWVGSL 

       370 
VKQHKEALKT KTH

Q9N119 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