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Database: UniProt
Entry: A7RLW5_NEMVE
LinkDB: A7RLW5_NEMVE
Original site: A7RLW5_NEMVE 
ID   A7RLW5_NEMVE            Unreviewed;       329 AA.
AC   A7RLW5;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=NEMVEDRAFT_v1g228294 {ECO:0000313|EMBL:EDO47406.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO47406.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO47406.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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; DS469519; EDO47406.1; -; Genomic_DNA.
DR   RefSeq; XP_001639469.1; XM_001639419.1.
DR   AlphaFoldDB; A7RLW5; -.
DR   STRING; 45351.A7RLW5; -.
DR   EnsemblMetazoa; EDO47406; EDO47406; NEMVEDRAFT_v1g228294.
DR   GeneID; 5519669; -.
DR   KEGG; nve:5519669; -.
DR   eggNOG; KOG0025; Eukaryota.
DR   HOGENOM; CLU_026673_17_1_1; -.
DR   InParanoid; A7RLW5; -.
DR   OMA; YGYTQSK; -.
DR   OrthoDB; 6213at2759; -.
DR   PhylomeDB; A7RLW5; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
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:UP000001593};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          9..326
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   329 AA;  35905 MW;  827CA06F79E000CD CRC64;
     MYKEYGDPGK VLSLEFVDRE VIGPSSVGVQ MVAAPVNPSD INMIQGSYAI KPALPAVGGN
     EGCGQVIKMG KEVKGVKEGD FVILAESGLG SWTRYHVLSE DQVIKVPDYI SVEMAATLSV
     NPCTAYRMLK DFEHLKPGDT VIQNGGNSGV GRAVIQLAAA WGIKTVNIVR DRPNLDVMVK
     ELTDLGATHV VTEDFCRTPE MANFMKDLRP VKLGLNCVGG KSATEVTRQL SDQGSIVTYG
     GMSKKPFLVP TGQLIFKDIR VRGFWMTAWN KHNTKSSERV SMIDEICQLH KDGKFSPPPC
     NKHALEHFQE AVGAAMQQYS TAKQLLTMT
//
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