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H17B6_BOVIN
ID   H17B6_BOVIN             Reviewed;         317 AA.
AC   Q3T001;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=17-beta-hydroxysteroid dehydrogenase type 6;
DE            Short=17-beta-HSD 6;
DE            Short=17-beta-HSD6;
DE            EC=1.1.1.105 {ECO:0000250|UniProtKB:Q9R092};
DE            EC=1.1.1.209 {ECO:0000250|UniProtKB:Q9R092};
DE            EC=1.1.1.239 {ECO:0000250|UniProtKB:Q9R092};
DE            EC=1.1.1.53 {ECO:0000250|UniProtKB:Q9R092};
DE            EC=1.1.1.62 {ECO:0000250|UniProtKB:Q9R092};
DE   AltName: Full=3-alpha->beta-hydroxysteroid epimerase;
DE            Short=3-alpha->beta-HSE;
DE   AltName: Full=Oxidative 3-alpha hydroxysteroid dehydrogenase;
DE   Flags: Precursor;
GN   Name=HSD17B6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NAD-dependent oxidoreductase with broad substrate specificity
CC       that shows both oxidative and reductive activity (in vitro). Has 17-
CC       beta-hydroxysteroid dehydrogenase activity towards various steroids (in
CC       vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone
CC       and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid
CC       dehydrogenase activity towards androsterone (in vitro). Has retinol
CC       dehydrogenase activity towards all-trans-retinol (in vitro). Can
CC       convert androsterone to epi-androsterone. Androsterone is first
CC       oxidized to 5-alpha-androstane-3,17-dione and then reduced to epi-
CC       andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids (By
CC       similarity). {ECO:0000250|UniProtKB:Q9R092}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-
CC         trans-retinal--[retinol-binding protein] + H(+) + NADH;
CC         Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC         EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:Q9R092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH;
CC         Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.105; Evidence={ECO:0000250|UniProtKB:Q9R092};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285;
CC         Evidence={ECO:0000250|UniProtKB:Q9R092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3alpha-hydroxy-5alpha-androstan-17-one + NAD(+) = 5alpha-
CC         androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:20381,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.209;
CC         Evidence={ECO:0000250|UniProtKB:Q9R092};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20382;
CC         Evidence={ECO:0000250|UniProtKB:Q9R092};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20383;
CC         Evidence={ECO:0000250|UniProtKB:Q9R092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) +
CC         NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422,
CC         ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.239; Evidence={ECO:0000250|UniProtKB:Q9R092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-
CC         hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53;
CC         Evidence={ECO:0000250|UniProtKB:Q9R092};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006;
CC         Evidence={ECO:0000250|UniProtKB:Q9R092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH;
CC         Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9R092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62;
CC         Evidence={ECO:0000250|UniProtKB:Q9R092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3alpha-hydroxy-5alpha-pregnan-20-one + NAD(+) = 5alpha-
CC         pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41980,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:50169,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000250|UniProtKB:O14756};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41981;
CC         Evidence={ECO:0000250|UniProtKB:O14756};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-androstane-3beta,17beta-diol + NAD(+) = 17beta-hydroxy-
CC         5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42184,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         Evidence={ECO:0000250|UniProtKB:O14756};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42186;
CC         Evidence={ECO:0000250|UniProtKB:O14756};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3beta-hydroxy-5alpha-androstan-17-one + NAD(+) = 5alpha-
CC         androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:42188,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:541975;
CC         Evidence={ECO:0000250|UniProtKB:O14756};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42190;
CC         Evidence={ECO:0000250|UniProtKB:O14756};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000250|UniProtKB:O14756}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O14756}; Lumenal side
CC       {ECO:0000250|UniProtKB:O14756}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O14756}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O14756}; Lumenal side
CC       {ECO:0000250|UniProtKB:O14756}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; BC102626; AAI02627.1; -; mRNA.
DR   RefSeq; NP_001030472.1; NM_001035395.2.
DR   AlphaFoldDB; Q3T001; -.
DR   SMR; Q3T001; -.
DR   STRING; 9913.ENSBTAP00000015564; -.
DR   PaxDb; Q3T001; -.
DR   PeptideAtlas; Q3T001; -.
DR   GeneID; 533086; -.
DR   KEGG; bta:533086; -.
DR   CTD; 8630; -.
DR   eggNOG; KOG1610; Eukaryota.
DR   InParanoid; Q3T001; -.
DR   OrthoDB; 1390068at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR   GO; GO:0047024; F:5alpha-androstane-3beta,17beta-diol dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0047044; F:androstan-3-alpha,17-beta-diol dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0047023; F:androsterone dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0004745; F:NAD-retinol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047045; F:testosterone 17-beta-dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0062175; P:brexanolone catabolic process; ISS:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Lipid metabolism; Membrane; Microsome;
KW   NAD; Oxidoreductase; Reference proteome; Signal; Steroid metabolism.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..317
FT                   /note="17-beta-hydroxysteroid dehydrogenase type 6"
FT                   /id="PRO_0000303210"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         33..57
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   317 AA;  36198 MW;  4B1A2ED7906FBB12 CRC64;
     MWLYLAVLLG LYYLLRWFRE RQVVSHLQDK FVFITGCDSG FGNQLARQLD LRGLRVLAGC
     LTEQGAEQLR NQTSDRLQTV ILDVTKTESI AAATEWVKEC VGDRGLWGLV NNAGIFHSHG
     YAEWIKIETY RDTLRVNLIG VIEVTLSMLP LVRKAQGRIV NVSSILGRIA FFGAVYSCSK
     YGVEAFSDIL RRELQHFGVK VSMVEPGYFR TAMTDWQKFS EIMKQIWKET PAHIKETYGQ
     KFFDAYHDLM KQGLLSCSTN LNLVTDCMEH ALTSVHPRTR YSAGWDAQFF FVPLSYLPTS
     LADYILTRSW PKPAQAV
 
 
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