HSD_MYCTO
ID HSD_MYCTO Reviewed; 260 AA.
AC P9WGT0; L0TB81; P69167; Q10855;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase {ECO:0000250|UniProtKB:P9WGT1};
DE EC=1.1.1.53 {ECO:0000250|UniProtKB:P9WGT1};
GN Name=fabG3; OrderedLocusNames=MT2058;
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: Probably involved in steroid metabolism.
CC {ECO:0000250|UniProtKB:P9WGT1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androstan-3alpha,17beta-diol + NAD(+) = 17beta-
CC hydroxyandrostanone + H(+) + NADH; Xref=Rhea:RHEA:22400,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18011, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:85278; EC=1.1.1.53;
CC Evidence={ECO:0000250|UniProtKB:P9WGT1};
CC -!- PATHWAY: Lipid metabolism; steroid degradation.
CC {ECO:0000250|UniProtKB:P9WGT1}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P9WGT1}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46335.1; -; Genomic_DNA.
DR PIR; H70758; H70758.
DR RefSeq; WP_003899124.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGT0; -.
DR SMR; P9WGT0; -.
DR EnsemblBacteria; AAK46335; AAK46335; MT2058.
DR KEGG; mtc:MT2058; -.
DR PATRIC; fig|83331.31.peg.2215; -.
DR HOGENOM; CLU_010194_1_0_11; -.
DR UniPathway; UPA00722; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006706; P:steroid catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Lipid metabolism; NAD; Oxidoreductase; Steroid metabolism.
FT CHAIN 1..260
FT /note="3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase"
FT /id="PRO_0000428308"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 17..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 61..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 183..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
SQ SEQUENCE 260 AA; 27000 MW; 1C74F55B87623A77 CRC64;
MSGRLIGKVA LVSGGARGMG ASHVRAMVAE GAKVVFGDIL DEEGKAVAAE LADAARYVHL
DVTQPAQWTA AVDTAVTAFG GLHVLVNNAG ILNIGTIEDY ALTEWQRILD VNLTGVFLGI
RAVVKPMKEA GRGSIINISS IEGLAGTVAC HGYTATKFAV RGLTKSTALE LGPGGIRVNS
IHPGLVKTPM TDWVPEDIFQ TALGRAAEPV EVSNLVVYLA SDESSYSTGA EFVVDGGTVA
GLAHNDFGAV EVSSQPEWVT