ID B7X8I1_GLARU Unreviewed; 320 AA.
AC B7X8I1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=3-ketoacyl-CoA reductase {ECO:0000256|ARBA:ARBA00041250};
DE EC=1.1.1.330 {ECO:0000256|ARBA:ARBA00039105};
DE EC=1.1.1.62 {ECO:0000256|ARBA:ARBA00024072};
GN Name=17-beta HSD type12 {ECO:0000313|EMBL:BAH09095.1};
OS Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Glandirana.
OX NCBI_TaxID=8410 {ECO:0000313|EMBL:BAH09095.1};
RN [1] {ECO:0000313|EMBL:BAH09095.1}
RP NUCLEOTIDE SEQUENCE.
RA Suda M., Nakamura M.;
RT "Rana rugosa mRNA for 17-beta HSD type12, complete cds.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the second of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of two carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has
CC a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-
CC hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby,
CC it may participate in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. May also catalyze
CC the transformation of estrone (E1) into estradiol (E2) and play a role
CC in estrogen formation. {ECO:0000256|ARBA:ARBA00037337}.
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:0000256|ARBA:ARBA00035946};
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:0000256|ARBA:ARBA00036215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-
CC long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330;
CC Evidence={ECO:0000256|ARBA:ARBA00036602};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037929}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 17-beta-HSD 3 subfamily. {ECO:0000256|ARBA:ARBA00038261}.
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DR EMBL; AB372020; BAH09095.1; -; mRNA.
DR AlphaFoldDB; B7X8I1; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd05356; 17beta-HSD1_like_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43899; RH59310P; 1.
DR PANTHER; PTHR43899:SF14; VERY-LONG-CHAIN 3-OXOACYL-COA REDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PIRSF; PIRSF000126; 11-beta-HSD1; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022955};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 320 AA; 35242 MW; 610F5D2D9B9AE259 CRC64;
MVASEMLAGL PVPCARFFFY VGVLAASWWG VRAAWRLLSA VRVWGLGRGT QVGPGLGKWA
VVTGATDGIG KAYAEELARR GMSIVLISRS QDKLDEVAKN IREKFKVETK VIAADFGKPA
EIYERIEVGL KSLEIGVLVN NVGVSYEYPE YFLDIPDLDN TLDMLININI TSVCKMTRLV
MPGMLERSKG VILNISSASG MYPVPLLTVY SATKAFVDFF SRGLQAEYRN KGITVQSVLP
FFVATKLSKI RKPTWDKPSP EHYVRSALNT VGLQTRTNAT CHALMGWVTG SVLPSCLATK
LAMNVNKGLR ARFLKRAKKN
//
