HSD_STREX
ID HSD_STREX Reviewed; 255 AA.
AC P19992;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase;
DE EC=1.1.1.53;
OS Streptomyces exfoliatus (Streptomyces hydrogenans).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1905;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2194840; DOI=10.1016/0014-5793(90)81504-h;
RA Marekov L., Krook M., Joernvall H.;
RT "Prokaryotic 20 beta-hydroxysteroid dehydrogenase is an enzyme of the
RT 'short-chain, non-metalloenzyme' alcohol dehydrogenase type.";
RL FEBS Lett. 266:51-54(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=1946424; DOI=10.1073/pnas.88.22.10064;
RA Ghosh D., Weeks C.M., Grochulski P., Duax W.L., Erman M., Rimsay R.L.,
RA Orr J.C.;
RT "Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid
RT dehydrogenase: a member of a short-chain dehydrogenase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10064-10068(1991).
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 -!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR PIR; S10707; S10707.
DR PDB; 1HDC; X-ray; 2.20 A; A/B/C/D=2-255.
DR PDB; 2HSD; X-ray; 2.64 A; A/B/C/D=2-255.
DR PDBsum; 1HDC; -.
DR PDBsum; 2HSD; -.
DR AlphaFoldDB; P19992; -.
DR SMR; P19992; -.
DR ChEMBL; CHEMBL3243917; -.
DR DrugBank; DB02329; Carbenoxolone.
DR UniPathway; UPA00229; -.
DR EvolutionaryTrace; P19992; -.
DR GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008207; P:C21-steroid hormone metabolic 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lipid metabolism; NAD;
KW Oxidoreductase; Steroid metabolism.
FT CHAIN 1..255
FT /note="3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase"
FT /id="PRO_0000054713"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT BINDING 10..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1HDC"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:1HDC"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:1HDC"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:1HDC"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:1HDC"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 150..170
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1HDC"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:1HDC"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1HDC"
FT TURN 241..245
FT /evidence="ECO:0007829|PDB:1HDC"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:1HDC"
SQ SEQUENCE 255 AA; 26484 MW; 9CB93CB66AA628D5 CRC64;
MNDLSGKTVI ITGGARGLGA EAARQAVAAG ARVVLADVLD EEGAATAREL GDAARYQHLD
VTIEEDWQRV VAYAREEFGS VDGLVNNAGI STGMFLETES VERFRKVVDI NLTGVFIGMK
TVIPAMKDAG GGSIVNISSA AGLMGLALTS SYGASKWGVR GLSKLAAVEL GTDRIRVNSV
HPGMTYTPMT AETGIRQGEG NYPNTPMGRV GNEPGEIAGA VVKLLSDTSS YVTGAELAVD
GGWTTGPTVK YVMGQ