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

From

Bos taurus (Bovine)

[TaxID: 9913]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Ovary; DOI=10.1016/0014-5793(89)81516-9; PubMed=2599102 [NCBI, ExPASy, EBI, Israel, Japan] Zhao H.-F., Simard J., Labrie C., Breton N., Rheaume E., Luu-The V., Labrie F.; "Molecular cloning, cDNA structure and predicted amino acid sequence of bovine 3 beta-hydroxy-5-ene steroid dehydrogenase/delta 5-delta 4 isomerase."; FEBS Lett. 259:153-157(1989).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Liver; NIH - Mammalian Gene Collection (MGC) project; Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[3]	PARTIAL PROTEIN SEQUENCE. TISSUE=Adrenal gland; DOI=10.1021/bi00247a003; PubMed=1868086 [NCBI, ExPASy, EBI, Israel, Japan] Rutherfurd K.J., Chen S., Shively J.E.; "Isolation and amino acid sequence analysis of bovine adrenal 3 beta-hydroxysteroid dehydrogenase/steroid isomerase."; Biochemistry 30:8108-8116(1991).

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

X17614; CAA35615.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111203; AAI11204.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S07102; DEBOHS.

NP_776768.1; -.

3D structure databases

ModBase

P14893.

Ontologies

GO:0030868;	Cellular component: smooth endoplasmic reticulum membrane (inferred from direct assay from UniProtKB).
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.

BLOCKS

P14893.

Genome annotation databases

Ensembl

ENSBTAG00000006769; Bos taurus. [Contig view]

GeneID

281824; -.

KEGG

bta:281824; -.

Phylogenomic databases

HOVERGEN

P14893; -.

Other

ProtoNet

P14893.

UniRef

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

Keywords

Direct protein sequencing; 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.`
`CHAIN`	`2 373`	`372`	`3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase.`	`PRO_0000087771`
`TRANSMEM`	`288 308`	`21`	`Potential.`

Sequence information

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

Molecular weight: 42220 Da [This is the MW of the unprocessed precursor]

CRC64: B9BDB817E7B5A1D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGWSCLVTG GGGFLGQRII CLLVEEKDLQ EIRVLDKVFR PEVREEFSKL QSKIKLTLLE 

        70         80         90        100        110        120 
GDILDEQCLK GACQGTSVVI HTASVIDVRN AVPRETIMNV NVKGTQLLLE ACVQASVPVF 

       130        140        150        160        170        180 
IHTSTIEVAG PNSYREIIQD GREEEHHESA WSSPYPYSKK LAEKAVLGAN GWALKNGGTL 

       190        200        210        220        230        240 
YTCALRPMYI YGEGSPFLSA YMHGALNNNG ILTNHCKFSR VNPVYVGNVA WAHILALRAL 

       250        260        270        280        290        300 
RDPKKVPNIQ GQFYYISDDT PHQSYDDLNY TLSKEWGFCL DSRMSLPISL QYWLAFLLEI 

       310        320        330        340        350        360 
VSFLLSPIYK YNPCFNRHLV TLSNSVFTFS YKKAQRDLGY EPLYTWEEAK QKTKEWIGSL 

       370 
VKQHKETLKT KIH

P14893 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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