Reviewed, UniProtKB/Swiss-Prot Q9N119 (3BHS_PIG)

Names and origin

Protein names

Recommended name:
    3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase
      Short name=3-beta-HSD
Including the following 2 domains:
    1- Recommended name:
            3-beta-hydroxy-Delta(5)-steroid dehydrogenase
              EC=1.1.1.145
        Alternative name(s):
            3-beta-hydroxy-5-ene steroid dehydrogenase
            Progesterone reductase
    2- Recommended name:
            Steroid Delta-isomerase
              EC=5.3.3.1
        Alternative name(s):
            Delta-5-3-ketosteroid isomerase

Gene names

Name:	HSD3B
Synonyms:	3b-HSD

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	373 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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-Delta(5)-steroid + NAD+ = a 3-oxo-Delta(5)-steroid + NADH. A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid.
Pathway	Lipid metabolism; steroid biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Sequence similarities	Belongs to the 3-beta-HSD family.

Ontologies

Keywords
Biological process	Steroidogenesis
Cellular component	Endoplasmic reticulum Membrane Mitochondrion
Domain	Transmembrane
Ligand	NAD
Molecular function	Isomerase Oxidoreductase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-beta-hydroxy-delta5-steroid dehydrogenase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro steroid delta-isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity UniProtKB P14893
	Chain	2 – 373	372	3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase		PRO_0000087786
Regions
	Transmembrane	292 – 309	18	Potential
Sites
	Active site	155	1	Proton acceptor By similarity
	Binding site	159	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9N119-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 8BD4FEEF0117F6FF	FASTA	373	41,882
	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

References

[1]	"cDNA cloning and physical mapping of porcine 3 beta-hydroxysteroid dehydrogenase/Delta 5-delta 4 isomerase." von Teichman A., Joerg H., Werner P., Brenig B., Stranzinger G. Anim. Genet. 32:298-302(2001) [PubMed: 11683717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Adipose tissue.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF232699 mRNA. Translation: AAF37295.2.
RefSeq	NP_001004049.1.
UniGene	Ssc.14393
3D structure databases
SMR	Q9N119. Positions 5-364.
ModBase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000007360; ENSSSCP00000007165; ENSSSCG00000006719; Sus scrofa. [Genome view]
GeneID	445539.
KEGG	ssc:445539.
Organism-specific databases
CTD	445539.
Phylogenomic databases
HOVERGEN	Q9N119.
Enzyme and pathway databases
BRENDA	1.1.1.145. 249. 5.3.3.1. 249.
Family and domain databases
InterPro	IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3BHS_PIG

Accession

Primary (citable) accession number: Q9N119

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 56 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)