ID 3BHS1_MACMU Reviewed; 373 AA. AC P27365; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 25-NOV-2008, entry version 62. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1; DE Short=3-beta-HSD I; DE Includes: DE RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.145; DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase; DE AltName: Full=Progesterone reductase; DE Includes: DE RecName: Full=Steroid Delta-isomerase; DE EC=5.3.3.1; DE AltName: Full=Delta-5-3-ketosteroid isomerase; GN Name=HSD3B1; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RX MEDLINE=91267292; PubMed=2050270; DOI=10.1016/0303-7207(91)90224-G; RA Simard J., Melner M.H., Breton N., Low K.G., Zhao H.-F., Periman L.M., RA Labrie F.; RT "Characterization of macaque 3 beta-hydroxy-5-ene steroid RT dehydrogenase/delta 5-delta 4 isomerase: structure and expression in RT steroidogenic and peripheral tissues in primate."; RL Mol. Cell. Endocrinol. 75:101-110(1991). CC -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and CC the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic CC system plays a crucial role in the biosynthesis of all classes of CC hormonal steroids. CC -!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a CC 3-oxo-Delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- CC steroid. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Mitochondrion membrane; Single-pass membrane CC protein. CC -!- TISSUE SPECIFICITY: Adrenal glands, testes and ovaries. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M67467; AAA36847.1; -; mRNA. DR PIR; A54325; A54325. DR RefSeq; XP_001113717.1; -. DR RefSeq; XP_001113744.1; -. DR RefSeq; XP_001113769.1; -. DR UniGene; Mmu.15109; -. DR Ensembl; ENSMMUG00000016568; Macaca mulatta. DR GeneID; 712686; -. DR HOVERGEN; P27365; -. DR LinkHub; P27365; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase...; IEA:InterPro. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:EC. DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR002225; 3Beta_OHSteriod_DHase/Estase. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01073; 3Beta_HSD; 1. PE 2: Evidence at transcript level; KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; KW Transmembrane. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 373 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type 1. FT /FTId=PRO_0000087776. FT TRANSMEM 288 308 Potential. SQ SEQUENCE 373 AA; 42005 MW; 9B6C172F319B5BB9 CRC64; MTGWSCLVTG AGGFLGQRIV RLLVEEKELK EIRVLDKAFR PELREEFSKL QNKTKLTVLE GDILDEPFLK RACQDVSVVI HTACIIDVFG VTHRESIMNV NVKGTQLLLE ACVQASVPVF IYTSTLEVAG PNSYKEIIQN GHEEEPLENT WPAPYPYSKK LAEKAVLAAN GWTLKNGGTL YTCALRPMYI YGEGGPFLSA SINEALNNNG ILSSVGKFST VNPVYVGNVA WAHILALRAL RDPKKAPSVQ GQFYYISDDT PHQSYDNLNY ILSKEFGLCL DSRWSLPLAL MYWIGFLLEV VSFLLSPVYS YQPPFNRHTV TLSNSVFTFS YKKAQRDLAY KPLYSWEEAK QKTVEWVGSL VDRHKETLKS KTQ //