ID T1K9K4_TETUR Unreviewed; 343 AA.
AC T1K9K4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=107361729 {ECO:0000313|EnsemblMetazoa:tetur07g05260.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur07g05260.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur07g05260.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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; CAEY01001892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015784087.1; XM_015928601.1.
DR AlphaFoldDB; T1K9K4; -.
DR STRING; 32264.T1K9K4; -.
DR EnsemblMetazoa; tetur07g05260.1; tetur07g05260.1; tetur07g05260.
DR GeneID; 107361729; -.
DR KEGG; tut:107361729; -.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_1_1; -.
DR OMA; AWVLMER; -.
DR OrthoDB; 6213at2759; -.
DR Proteomes; UP000015104; 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:UP000015104};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 21..339
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 343 AA; 37218 MW; AF103408C83DD554 CRC64;
MSFSLVLKNK GPLAQAIEKV DTSSSVNLEA TLKDNEVLIQ FIASAINPSD VGVIEGWYPS
AAELPLVPGN EGVAKVLKVG PGVSKLAVGD HVIPGKGLFG TWRTHAIASE NDLLSIDKDL
DIYTAAQIMV NPPTAYRMLK DFVTLKPGDC VMQNGANSAV GLLVIQLCKA WGYKTINVVR
ARPNPDDMAK LVSKLTEYGA DHVVTEEDIA NDEAMNEIWS SGTPKPILAF ECIGGENANN
CIRHLADEAT MVIYGTMTKK PIEVPAGPTI FKQLRFVGFW LAKVYRGNPE EYLRMSAELV
SMFKSGQLKA PKVVPVKMVD YLEAFEKSTN GFSEGKVVLT TEV
//
