3BHS_MYCTO
ID 3BHS_MYCTO Reviewed; 370 AA.
AC P9WQP6; L0T7C3; O53454; Q7D8U6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase;
DE AltName: Full=Cholesterol dehydrogenase;
DE Includes:
DE RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase;
DE Short=3-beta-HSD;
DE Short=3BHSD;
DE EC=1.1.1.145 {ECO:0000250|UniProtKB:P9WQP7};
DE AltName: Full=3-beta hydroxysterol dehydrogenase;
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 {ECO:0000250|UniProtKB:P9WQP7};
DE AltName: Full=Delta-5-3-ketosteroid isomerase;
GN OrderedLocusNames=MT1137;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the
CC oxidation and isomerization of cholesterol, pregnenolone, and
CC dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone,
CC and androsterone, respectively. {ECO:0000250|UniProtKB:P9WQP7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-
CC steroid + H(+) + NADH; Xref=Rhea:RHEA:24076, ChEBI:CHEBI:1722,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47907, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.145;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol + NAD(+) = cholest-5-en-3-one + H(+) + NADH;
CC Xref=Rhea:RHEA:35459, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:63906;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35460;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + pregnenolone = H(+) + NADH + pregn-5-ene-3,20-dione;
CC Xref=Rhea:RHEA:43924, ChEBI:CHEBI:15378, ChEBI:CHEBI:16581,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:63837;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43925;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxyandrost-5-en-17-one + NAD(+) = androst-5-ene-
CC 3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:43932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28689, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:83865; EC=1.1.1.145;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43933;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid;
CC Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909;
CC EC=5.3.3.1; Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholest-5-en-3-one = cholest-4-en-3-one; Xref=Rhea:RHEA:32187,
CC ChEBI:CHEBI:16175, ChEBI:CHEBI:63906; EC=5.3.3.1;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32188;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pregn-5-ene-3,20-dione = progesterone; Xref=Rhea:RHEA:43928,
CC ChEBI:CHEBI:17026, ChEBI:CHEBI:63837;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43929;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
CC Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
CC Evidence={ECO:0000250|UniProtKB:P9WQP7};
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR EMBL; AE000516; AAK45394.1; -; Genomic_DNA.
DR PIR; H70897; H70897.
DR RefSeq; WP_003405840.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQP6; -.
DR SMR; P9WQP6; -.
DR EnsemblBacteria; AAK45394; AAK45394; MT1137.
DR GeneID; 45425080; -.
DR KEGG; mtc:MT1137; -.
DR PATRIC; fig|83331.31.peg.1229; -.
DR HOGENOM; CLU_007383_6_8_11; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Isomerase; Lipid degradation; Lipid metabolism;
KW Multifunctional enzyme; NAD; Oxidoreductase; Steroid metabolism.
FT CHAIN 1..370
FT /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT isomerase"
FT /id="PRO_0000426739"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ 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