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3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (Cholesterol dehydrogenase) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (3-beta-HSD) (3BHSD) (EC 1.1.1.145) (3-beta hydroxysterol dehydrogenase) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)]

 3BHS_MYCTU              Reviewed;         370 AA.
P9WQP7; L0T7C3; O53454; Q7D8U6;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 28.
RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase;
AltName: Full=Cholesterol dehydrogenase;
Includes:
RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase;
Short=3-beta-HSD;
Short=3BHSD;
EC=1.1.1.145;
AltName: Full=3-beta hydroxysterol dehydrogenase;
AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase;
AltName: Full=Progesterone reductase;
Includes:
RecName: Full=Steroid Delta-isomerase;
EC=5.3.3.1;
AltName: Full=Delta-5-3-ketosteroid isomerase;
OrderedLocusNames=Rv1106c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION AS A 3BETA-HYDROXYSTEROL DEHYDROGENASE AND ISOMERASE,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION,
DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=17630785; DOI=10.1021/bi700688x;
Yang X., Dubnau E., Smith I., Sampson N.S.;
"Rv1106c from Mycobacterium tuberculosis is a 3beta-hydroxysteroid
dehydrogenase.";
Biochemistry 46:9058-9067(2007).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the
oxidation and isomerization of cholesterol, pregnenolone, and
dehydroepiandrosterone (DHEA) into cholest-4-en-3-one,
progesterone, and androsterone, respectively.
{ECO:0000269|PubMed:17630785}.
-!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a
3-oxo-Delta(5)-steroid + NADH. {ECO:0000269|PubMed:17630785}.
-!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-
steroid. {ECO:0000269|PubMed:17630785}.
-!- ENZYME REGULATION: Inhibited by EDTA, zinc, silver, copper, and
activated by magnesium and calcium. A competitive inhibition is
observed with NAD at concentrations higher than 5.6 mM, and with
trilostane (3,17-dihydroxy-4,5-epoxyandrost-2-ene-2-carbonitrile).
{ECO:0000269|PubMed:17630785}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is between 8.5-9.5. No catalytic activity is detected
below pH 7.5. {ECO:0000269|PubMed:17630785};
-!- PATHWAY: Lipid metabolism; steroid biosynthesis.
-!- SUBUNIT: Monomer. {ECO:0000305|PubMed:17630785}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17630785}.
-!- DISRUPTION PHENOTYPE: Disruption reduces the cholesterol oxidation
activity at least 90-fold. {ECO:0000269|PubMed:17630785}.
-!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP43859.1; -; Genomic_DNA.
PIR; H70897; H70897.
RefSeq; NP_215622.1; NC_000962.3.
RefSeq; WP_003405840.1; NZ_KK339370.1.
ProteinModelPortal; P9WQP7; -.
STRING; 83332.Rv1106c; -.
BindingDB; P9WQP7; -.
ChEMBL; CHEMBL1744528; -.
SwissLipids; SLP:000001012; -.
PaxDb; P9WQP7; -.
EnsemblBacteria; CCP43859; CCP43859; Rv1106c.
GeneID; 886004; -.
KEGG; mtu:Rv1106c; -.
TubercuList; Rv1106c; -.
eggNOG; ENOG4107RYV; Bacteria.
eggNOG; COG0451; LUCA.
KO; K16045; -.
OMA; HYYSCER; -.
PhylomeDB; P9WQP7; -.
BioCyc; MetaCyc:G185E-5271-MONOMER; -.
UniPathway; UPA00062; -.
PRO; PR:P9WQP7; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IDA:MTBBASE.
GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0070403; F:NAD+ binding; IDA:MTBBASE.
GO; GO:0004769; F:steroid delta-isomerase activity; IDA:MTBBASE.
GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008202; P:steroid metabolic process; IDA:MTBBASE.
InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF01073; 3Beta_HSD; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Isomerase; Lipid degradation;
Lipid metabolism; Multifunctional enzyme; NAD; Oxidoreductase;
Reference proteome; Steroid metabolism.
CHAIN 1 370 3 beta-hydroxysteroid dehydrogenase/Delta
5-->4-isomerase.
/FTId=PRO_0000403957.
ACT_SITE 158 158 Proton acceptor. {ECO:0000250}.
BINDING 162 162 NAD. {ECO:0000250}.
SEQUENCE 370 AA; 40742 MW; B2A93EC32AFEEA0B CRC64;
MLRRMGDASL TTELGRVLVT GGAGFVGANL VTTLLDRGHW VRSFDRAPSL LPAHPQLEVL
QGDITDADVC AAAVDGIDTI FHTAAIIELM GGASVTDEYR QRSFAVNVGG TENLLHAGQR
AGVQRFVYTS SNSVVMGGQN IAGGDETLPY TDRFNDLYTE TKVVAERFVL AQNGVDGMLT
CAIRPSGIWG NGDQTMFRKL FESVLKGHVK VLVGRKSARL DNSYVHNLIH GFILAAAHLV
PDGTAPGQAY FINDAEPINM FEFARPVLEA CGQRWPKMRI SGPAVRWVMT GWQRLHFRFG
FPAPLLEPLA VERLYLDNYF SIAKARRDLG YEPLFTTQQA LTECLPYYVS LFEQMKNEAR
AEKTAATVKP


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