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

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. 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. 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) [Complete proteome]

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 Transmembrane helix
Ligand	NAD
Molecular function	Isomerase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-beta-hydroxy-delta5-steroid dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide 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	Helical; Potential
Sites
	Active site	155	1	Proton acceptor By similarity
	Binding site	159	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9N119 [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. NM_001004049.1.
UniGene	Ssc.14393.
3D structure databases
ProteinModelPortal	Q9N119.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9N119.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000007360; ENSSSCP00000007165; ENSSSCG00000006719.
GeneID	445539.
KEGG	ssc:445539.
Organism-specific databases
CTD	3283.
Phylogenomic databases
GeneTree	ENSGT00550000074557.
HOVERGEN	HBG000014.
OMA	MAGWSCL.
OrthoDB	EOG4K3KWG.
Enzyme and pathway databases
BRENDA	1.1.1.145. 6170.
Family and domain databases
InterPro	IPR002225. 3Beta_OHSteriod_DH/Estase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00070.
Pfam	PF01073. 3Beta_HSD. 1 hit. [Graphical view]
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:	December 14, 2011
This is version 71 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program