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

Canis familiaris (Dog)

[TaxID: 9615]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Corpus luteum; Kowalewski M.P., Taubert A., Hoffmann B.; "Expression of 3-beta-hydroxysteroid dehydrogenase in canine corpus luteum during dioestrus."; Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
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 (By similarity). Mitochondrion membrane; Single-pass membrane protein (By similarity).
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

AY739720; AAW31741.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001010954.1; -.

UniGene

Cfa.13172

3D structure databases

ModBase

Q5IFP1.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
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

Q5IFP1.

Genome annotation databases

Ensembl

ENSCAFG00000010039; Canis familiaris. [Contig view]

GeneID

483146; -.

KEGG

cfa:483146; -.

Phylogenomic databases

HOVERGEN

Q5IFP1; -.

Other

ProtoNet

Q5IFP1.

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.`
`CHAIN`	`2 373`	`372`	`3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase.`	`PRO_0000087772`
`TRANSMEM`	`288 308`	`21`	`Potential.`

Sequence information

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

Molecular weight: 42378 Da [This is the MW of the unprocessed precursor]

CRC64: EB12CB016D650A5B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGWSCLVTG AGGFLGQRIV HLLAEEKELQ EIRALDKAFR PELLEEFSKL QSKTKLTMVE 

        70         80         90        100        110        120 
GDILDEQCLK RACQGTSVVI HTASVIDVMN VIHRETIMNV NLKGTQLLLE ACAQASVPIF 

       130        140        150        160        170        180 
IYTSTIEVAG PNSYRDIIQN AHEEEHLEST WSAPYPYSKK LAEKAVLAAN GWALKNGGTL 

       190        200        210        220        230        240 
HTCALRPMYI YGEGSIFLYN YIYKALRNNG ILTHHSKFSI VNPVYVGNVA WAHILALRAL 

       250        260        270        280        290        300 
QDPKKAPSVQ GQFYYISDDT PHQSYDDLNY NLSKEWGFSL DSRMSLPISL EYWLAFLLEI 

       310        320        330        340        350        360 
VSFLLSPIYK YQPPFNRHMV TLSNSIFTFS YKKAQRDLGY KPLFSWEEAK QKTTEWIGSL 

       370 
VKQHKETLKT KTH

Q5IFP1 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