O46516 (3BHS_HORSE) 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

Equus caballus (Horse) [Complete proteome]

Taxonomic identifier

9796 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

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
	Chain	2 – 373	372	3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase		PRO_0000087773
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)
	O46516 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 837A04E3C681417C	FASTA	373	42,411
	10 20 30 40 50 60 MAGWSCLVTG AGGFLGQRIV RLLVEEKEVQ EIRALDKVFR PELREEFSKL QSKVKLTVLE 70 80 90 100 110 120 GDILDEQFLK RACQGASAVI HTASIIDVTN LFNPQVTMNV NVEGTQLLLE ACSQASVPIF 130 140 150 160 170 180 IYTSSVAVAG PNSYREIIQN GHEEAHLETK WSSPYPYSKK LAEKAVLAAN GLPLKNGGTL 190 200 210 220 230 240 YTCALRPMFI YGEGSPTLYY LMHEGLNNNG ILTHNCKFSR ANPVYVGNIA WAHIMALRAL 250 260 270 280 290 300 RDPKKAPSIQ GQFYYISDDT PPQSYDDLTY TLSKKWGFCL DSRMRLPIFL KYWLAFLLEI 310 320 330 340 350 360 VSFLLSPIYK YRPPFDRHLV TWQNSVFTFS YKKAQRDMGY EPLFSWEEAK KRTTEWIDAL 370 VEPHQEALKT KTL

References

[1]	"Equine P450 cholesterol side-chain cleavage and 3 beta-hydroxysteroid dehydrogenase/delta(5)-delta(4) isomerase: molecular cloning and regulation of their messenger ribonucleic acids in equine follicles during the ovulatory process." Boerboom D., Sirois J. Biol. Reprod. 64:206-215(2001) [PubMed: 11133676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovarian follicle membrane.
[2]	"Molecular cloning, nucleotide sequence and tissue distribution of equine testicular 3 beta-hydroxysteroid dehydrogenase/delta5-delta4 isomerase messenger ribonucleic acid." Hasegawa T., Ishida M., Harigaya T., Ishida N., Mukoyama H. J. Equine Sci. 9:45-52(1998) Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF031665 mRNA. Translation: AAC04701.1. D89666 mRNA. Translation: BAA32698.1.
RefSeq	NP_001075380.1. NM_001081911.1.
UniGene	Eca.12081.
3D structure databases
ProteinModelPortal	O46516.
ModBase	Search...
Protein-protein interaction databases
STRING	O46516.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100034078.
KEGG	ecb:100034078.
Organism-specific databases
CTD	3283.
Phylogenomic databases
GeneTree	ENSGT00550000074557.
HOVERGEN	HBG000014.
InParanoid	O46516.
OrthoDB	EOG4K3KWG.
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_HORSE

Accession

Primary (citable) accession number: O46516
Secondary accession number(s): P79437

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program