ID A0A085NSU2_9BILA Unreviewed; 382 AA.
AC A0A085NSU2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial {ECO:0000256|ARBA:ARBA00041058};
DE EC=1.3.1.104 {ECO:0000256|ARBA:ARBA00038963};
DE AltName: Full=2-enoyl thioester reductase {ECO:0000256|ARBA:ARBA00042123};
GN ORFNames=M513_04024 {ECO:0000313|EMBL:KFD55106.1}, M514_04024
GN {ECO:0000313|EMBL:KFD72538.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD72538.1};
RN [1] {ECO:0000313|EMBL:KFD72538.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD72538.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD55106.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104;
CC Evidence={ECO:0000256|ARBA:ARBA00035831};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|ARBA:ARBA00010371}.
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DR EMBL; KL363202; KFD55106.1; -; Genomic_DNA.
DR EMBL; KL367477; KFD72538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085NSU2; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08290; ETR; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43981; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43981:SF2; ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 37..356
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 382 AA; 42023 MW; 291E8F9E9D5A30F6 CRC64;
MACFEMHVKL LNRFVRPKIN LFRTIVAQQL EYREHGDPPS VVKLTNHTLQ PIRADEVRYK
VMAATINPAD INTIQGIYPI KPPLPAVGGM EGVLRIEEVG SGVWDLAVGD WAIPSPAGFG
TWRTDGIAPR TDLIKISNKL SIVQAATLAV NPSTAYRMLK DFVDLTPGDV VIQNGANSAV
GQLVIQLCRH FNVSTVNLIR DGKADEKETK DYLGELGADV VLTETEFKRK VRSLFEKMAS
PKLALNCVSG RGIVYMAGCL APKGKLVTYG GMSKQPLHVP TGAFIFKEIQ LHGFWMTSWN
RDPANAVKRR KMLDVLTQLS LDGKLQPVKY QLVPFKEYQQ AIEATAAGHG RKKILVFEWC
ETLNGACCSA VNEAFSGSSV PC
//
