DHB8_CALJA
ID DHB8_CALJA Reviewed; 134 AA.
AC Q9GME3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Estradiol 17-beta-dehydrogenase 8;
DE EC=1.1.1.62;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 8;
DE Short=17-beta-HSD 8;
DE AltName: Full=3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit {ECO:0000250|UniProtKB:Q92506};
DE Short=KAR alpha subunit {ECO:0000250|UniProtKB:Q92506};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q92506};
DE AltName: Full=Testosterone 17-beta-dehydrogenase 8;
DE EC=1.1.1.239;
DE Flags: Fragment;
GN Name=HSD17B8;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11165027; DOI=10.1016/s0303-7207(00)00421-4;
RA Husen B., Adamski J., Rune G.M., Einspanier A.;
RT "Mechanisms of estradiol inactivation in primate endometrium.";
RL Mol. Cell. Endocrinol. 171:179-185(2001).
CC -!- FUNCTION: NAD-dependent 17-beta-hydroxysteroid dehydrogenase with
CC highest activity towards estradiol. Has very low activity towards
CC testosterone. The heterotetramer with CBR4 has NADH-dependent 3-
CC ketoacyl-acyl carrier protein reductase activity, and thereby plays a
CC role in mitochondrial fatty acid biosynthesis. Within the
CC heterotetramer, HSD17B8 binds NADH; CBR4 binds NADPD.
CC {ECO:0000250|UniProtKB:Q92506}.
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:Q92506};
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:Q92506};
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:Q92506};
CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC {ECO:0000250|UniProtKB:Q92506}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q92506}.
CC -!- SUBUNIT: Heterotetramer with CBR4; contains two molecules of HSD17B8
CC and CBR4. {ECO:0000250|UniProtKB:Q92506}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q92506}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF272012; AAG01114.1; -; mRNA.
DR AlphaFoldDB; Q9GME3; -.
DR SMR; Q9GME3; -.
DR STRING; 9483.ENSCJAP00000040269; -.
DR eggNOG; KOG1200; Eukaryota.
DR HOGENOM; CLU_010194_1_3_1; -.
DR InParanoid; Q9GME3; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00769; -.
DR Proteomes; UP000008225; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0106386; F:(3R)-hydroxyacyl-CoA dehydrogenase (NAD) activity; ISS:UniProtKB.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0070404; F:NADH binding; ISS:UniProtKB.
DR GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0006703; P:estrogen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis.
FT CHAIN <1..>134
FT /note="Estradiol 17-beta-dehydrogenase 8"
FT /id="PRO_0000054596"
FT ACT_SITE 51
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 51..55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 84..86
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT MOD_RES 42
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50171"
FT MOD_RES 55
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50171"
FT NON_TER 1
FT NON_TER 134
SQ SEQUENCE 134 AA; 13763 MW; 1D351CCF6D6181FF CRC64;
DWDKVIAVNL KGTFLVTQAA GQALVSSGCS GSIINISSIV GKVGNMGQTN YAASKAGVIG
LTQTAARELG RHGIRCNSVL PGFIATPMTQ KVPQKVMNKI TGMIPMGHLG DPEDVADVVA
FLASEDSGYI TGAS
