位置:首页 > 蛋白库 > 3BHS_MYCTU
3BHS_MYCTU
ID   3BHS_MYCTU              Reviewed;         370 AA.
AC   P9WQP7; 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 48.
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:0000269|PubMed:17630785};
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:0000269|PubMed:17630785};
DE     AltName: Full=Delta-5-3-ketosteroid isomerase;
GN   OrderedLocusNames=Rv1106c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION AS A 3BETA-HYDROXYSTEROL DEHYDROGENASE AND ISOMERASE, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, DISRUPTION
RP   PHENOTYPE, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=17630785; DOI=10.1021/bi700688x;
RA   Yang X., Dubnau E., Smith I., Sampson N.S.;
RT   "Rv1106c from Mycobacterium tuberculosis is a 3beta-hydroxysteroid
RT   dehydrogenase.";
RL   Biochemistry 46:9058-9067(2007).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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:0000269|PubMed:17630785}.
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:0000269|PubMed:17630785};
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:0000269|PubMed:17630785};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35460;
CC         Evidence={ECO:0000269|PubMed:17630785};
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:0000269|PubMed:17630785};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43925;
CC         Evidence={ECO:0000269|PubMed:17630785};
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:0000269|PubMed:17630785};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43933;
CC         Evidence={ECO:0000269|PubMed:17630785};
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:0000269|PubMed:17630785};
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:0000269|PubMed:17630785};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32188;
CC         Evidence={ECO:0000269|PubMed:17630785};
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:0000269|PubMed:17630785};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43929;
CC         Evidence={ECO:0000269|PubMed:17630785};
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:0000269|PubMed:17630785};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
CC         Evidence={ECO:0000269|PubMed:17630785};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA, zinc, silver, copper, and
CC       activated by magnesium and calcium. A competitive inhibition is
CC       observed with NAD at concentrations higher than 5.6 mM, and with
CC       trilostane (3,17-dihydroxy-4,5-epoxyandrost-2-ene-2-carbonitrile).
CC       {ECO:0000269|PubMed:17630785}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is between 8.5-9.5. No catalytic activity is detected
CC         below pH 7.5. {ECO:0000269|PubMed:17630785};
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:17630785}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17630785}.
CC   -!- DISRUPTION PHENOTYPE: Disruption reduces the cholesterol oxidation
CC       activity at least 90-fold. {ECO:0000269|PubMed:17630785}.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL123456; CCP43859.1; -; Genomic_DNA.
DR   PIR; H70897; H70897.
DR   RefSeq; NP_215622.1; NC_000962.3.
DR   RefSeq; WP_003405840.1; NZ_NVQJ01000021.1.
DR   AlphaFoldDB; P9WQP7; -.
DR   SMR; P9WQP7; -.
DR   STRING; 83332.Rv1106c; -.
DR   BindingDB; P9WQP7; -.
DR   ChEMBL; CHEMBL1744528; -.
DR   SwissLipids; SLP:000001012; -.
DR   PaxDb; P9WQP7; -.
DR   PRIDE; P9WQP7; -.
DR   DNASU; 886004; -.
DR   GeneID; 45425080; -.
DR   GeneID; 886004; -.
DR   KEGG; mtu:Rv1106c; -.
DR   TubercuList; Rv1106c; -.
DR   eggNOG; COG0451; Bacteria.
DR   OMA; WGPGDTQ; -.
DR   PhylomeDB; P9WQP7; -.
DR   BioCyc; MetaCyc:G185E-5271-MON; -.
DR   BRENDA; 1.1.1.145; 3445.
DR   UniPathway; UPA00062; -.
DR   PRO; PR:P9WQP7; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IDA:MTBBASE.
DR   GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070403; F:NAD+ binding; IDA:MTBBASE.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; IDA:MTBBASE.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IDA:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008202; P:steroid metabolic process; IDA:MTBBASE.
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   1: Evidence at protein level;
KW   Cytoplasm; Isomerase; Lipid degradation; Lipid metabolism;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome;
KW   Steroid metabolism.
FT   CHAIN           1..370
FT                   /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT                   isomerase"
FT                   /id="PRO_0000403957"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024