ID A0A0V1MZ80_9BILA Unreviewed; 434 AA.
AC A0A0V1MZ80;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 Name=Mecr {ECO:0000313|EMBL:KRZ77044.1};
GN ORFNames=T10_11541 {ECO:0000313|EMBL:KRZ77044.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77044.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ77044.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77044.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ77044.1}.
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DR EMBL; JYDO01000023; KRZ77044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MZ80; -.
DR STRING; 268474.A0A0V1MZ80; -.
DR Proteomes; UP000054843; 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 Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 113..432
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 434 AA; 48245 MW; FE8852FF05945FC8 CRC64;
MKNENCNETS FQASHLLSSY FQFIIFEIDK RIQFVFFLDS RTRLLSSMLV QSQQQSNQSG
ICSLVILDTL LAVVQQFSTL YTKMLFRCWL SAGSFVVHKR ALQSLQMVYA EYGDPSKVLH
ERTEELKPLS KGELRYKMLA ASINPSDINQ VQGVYPVKPP LPAVGGGDCV MKVEELGPEV
KEFQVGDWAI PSHPGFGAWR TCGITTPEHL IKVNNKLPAQ YAATLSVNPS TAYRMLKGYV
KLGAGDAVLQ NAANSAVGQL IIQLARHFGH KTVNIIRDKN DGGKTAEYLR SLGADYVVTD
TQFKEESKRI FGELGPPKLA LNCVSGRSTL YLAGALAPRG KLVTYGGMSK QALQIPSGAL
IFKNIQVLGF WLTDWDQKPE NRQQRIQMLD ELSELALSGK LKMPLYESVP FKDFGRAMEE
SLTGTGKKKM LVFD
//
