P14893 (3BHS_BOVIN) 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

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

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

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 protein 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 Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell smooth endoplasmic reticulum membrane Inferred from direct assay. Source: UniProtKB
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
	Chain	2 – 373	372	3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase		PRO_0000087771
Regions
	Transmembrane	288 – 308	21	Helical; Potential
Sites
	Active site	155	1	Proton acceptor By similarity
	Binding site	159	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P14893 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B9BDB817E7B5A1D1	FASTA	373	42,220
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, cDNA structure and predicted amino acid sequence of bovine 3 beta-hydroxy-5-ene steroid dehydrogenase/delta 5-delta 4 isomerase." Zhao H.-F., Simard J., Labrie C., Breton N., Rheaume E., Luu-The V., Labrie F. FEBS Lett. 259:153-157(1989) [PubMed: 2599102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver.
[3]	"Isolation and amino acid sequence analysis of bovine adrenal 3 beta-hydroxysteroid dehydrogenase/steroid isomerase." Rutherfurd K.J., Chen S., Shively J.E. Biochemistry 30:8108-8116(1991) [PubMed: 1868086] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Adrenal gland.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X17614 mRNA. Translation: CAA35615.1. BC111203 mRNA. Translation: AAI11204.2.
IPI	IPI00703764.
PIR	DEBOHS. S07102.
RefSeq	NP_776768.1. NM_174343.2.
UniGene	Bt.106555.
3D structure databases
ProteinModelPortal	P14893.
ModBase	Search...
Protein-protein interaction databases
STRING	P14893.
Proteomic databases
PRIDE	P14893.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000010992; ENSBTAP00000010992; ENSBTAG00000006769.
GeneID	281824.
KEGG	bta:281824.
Organism-specific databases
CTD	3283.
Phylogenomic databases
eggNOG	maNOG12250.
GeneTree	ENSGT00550000074557.
HOVERGEN	HBG000014.
InParanoid	P14893.
OrthoDB	EOG4K3KWG.
PhylomeDB	P14893.
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_BOVIN

Accession

Primary (citable) accession number: P14893
Secondary accession number(s): Q2T9Y8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program