LE767_CAEBR
ID LE767_CAEBR Reviewed; 316 AA.
AC Q60V51; A8XW80;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Very-long-chain 3-oxooacyl-coA reductase let-767;
DE EC=1.1.1.330;
DE AltName: Full=Lethal protein 767;
GN Name=let-767 {ECO:0000250|UniProtKB:Q09517}; ORFNames=CBG19695;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Required for branched chain fatty acid synthesis. Catalyzes
CC the reduction of the 3-ketoacyl-CoA intermediate that is formed in each
CC cycle of fatty acid elongation. Very long-chain fatty acids (VLCFAs)
CC serve as precursors for ceramide and sphingolipids. May also be
CC required for sterol hormone production (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q09517}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 17-beta-HSD 3 subfamily. {ECO:0000305}.
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DR EMBL; HE600934; CAP36899.1; -; Genomic_DNA.
DR RefSeq; XP_002634709.1; XM_002634663.1.
DR AlphaFoldDB; Q60V51; -.
DR SMR; Q60V51; -.
DR STRING; 6238.CBG19695; -.
DR EnsemblMetazoa; CBG19695.1; CBG19695.1; WBGene00038870.
DR GeneID; 8576702; -.
DR KEGG; cbr:CBG_19695; -.
DR CTD; 8576702; -.
DR WormBase; CBG19695; CBP04589; WBGene00038870; Cbr-let-767.
DR eggNOG; KOG1014; Eukaryota.
DR HOGENOM; CLU_010194_38_0_1; -.
DR InParanoid; Q60V51; -.
DR OMA; TIAPMMV; -.
DR OrthoDB; 895581at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0045179; C:apical cortex; IEA:EnsemblMetazoa.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IEA:EnsemblMetazoa.
DR GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IEA:EnsemblMetazoa.
DR GO; GO:0008209; P:androgen metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IEA:EnsemblMetazoa.
DR GO; GO:0008210; P:estrogen metabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR GO; GO:0030540; P:female genitalia development; ISS:UniProtKB.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:EnsemblMetazoa.
DR GO; GO:0042303; P:molting cycle; ISS:UniProtKB.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:EnsemblMetazoa.
DR GO; GO:0032350; P:regulation of hormone metabolic process; ISS:UniProtKB.
DR GO; GO:0000003; P:reproduction; ISS:UniProtKB.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NADP; Oxidoreductase; Reference proteome;
KW Steroid biosynthesis.
FT CHAIN 1..316
FT /note="Very-long-chain 3-oxooacyl-coA reductase let-767"
FT /id="PRO_0000280225"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00334,
FT ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 52..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00334"
FT BINDING 206
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 316 AA; 34423 MW; BB1BF86DA6204640 CRC64;
MACQCFLVGA GYVALAAVAY RILTIFSNIL GPYVLLSPID LKKRAGASWA VITGATDGIG
KAYAFELARR GFNVFIVSRT QSKLDETKKE ILEKYPNIEV RTAAYDFTNA APSGYKNLLE
TLNKVEIGVL VNNVGLSYEY PDVLHKVDGG IERLANITTI NTLPPTLLSA GILPQMVARK
AGVIVNVGSS ASANQMALWA VYSATKKYVS WLTAILRKEY EHQGITIQTI APMMVATKMS
KVKRTSFFTP DGATFAKSAL NTVGNSSDTT GYITHQLQLE VMDLIPTFIR DKILTNMSVG
TRAAALRKKE REAKAQ
