TER_EUGGR
ID TER_EUGGR Reviewed; 539 AA.
AC Q5EU90;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Trans-2-enoyl-CoA reductase {ECO:0000303|PubMed:15569691, ECO:0000303|PubMed:30650145};
DE Short=TER1 {ECO:0000303|PubMed:30650145};
DE EC=1.3.1.38 {ECO:0000269|PubMed:15569691, ECO:0000269|PubMed:30650145};
DE EC=1.3.1.44 {ECO:0000269|PubMed:15569691};
DE EC=1.3.1.86 {ECO:0000269|PubMed:15569691, ECO:0000269|PubMed:30650145};
DE Flags: Precursor;
GN Name=TER;
OS Euglena gracilis.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, BLOCKAGE OF N-TERMINUS, IDENTIFICATION BY
RP MASS SPECTROMETRY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND SUBUNIT.
RC STRAIN=SAG 1224-5/25;
RX PubMed=15569691; DOI=10.1074/jbc.m411010200;
RA Hoffmeister M., Piotrowski M., Nowitzki U., Martin W.;
RT "Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from
RT Euglena gracilis defines a new family of enzymes involved in lipid
RT synthesis.";
RL J. Biol. Chem. 280:4329-4338(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30650145; DOI=10.1371/journal.pone.0210755;
RA Tomiyama T., Goto K., Tanaka Y., Maruta T., Ogawa T., Sawa Y., Ito T.,
RA Ishikawa T.;
RT "A major isoform of mitochondrial trans-2-enoyl-CoA reductase is
RT dispensable for wax ester production in Euglena gracilis under anaerobic
RT conditions.";
RL PLoS ONE 14:e0210755-e0210755(2019).
CC -!- FUNCTION: Catalyzes reduction of trans-2-enoyl-CoA to acyl-CoA, an
CC important step in the fatty acid biosynthesis pathway, which is
CC performed in mitochondria under anaerobiosis. Preferably catalyzes the
CC reduction of short chain length substrates such as crotonyl-CoA ((2E)-
CC butenoyl-CoA) and (2E)-hexenoyl-CoA. Can use both NADH and NADPH as
CC electron donor, with 2-3-fold higher specific activities for NADH
CC relative to NADPH. Originally thought to contribute to wax ester
CC production under anaerobic conditions (PubMed:15569691). Later shown to
CC be dispensable for wax ester production under anaerobic conditions, but
CC involved in the greening process (chlorophyll synthesis and/or
CC chloroplast development) (PubMed:30650145).
CC {ECO:0000269|PubMed:15569691, ECO:0000269|PubMed:30650145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:18177, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.44;
CC Evidence={ECO:0000269|PubMed:15569691};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18179;
CC Evidence={ECO:0000269|PubMed:15569691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + NAD(+) = (2E)-butenoyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:52572, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:15569691};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:52574;
CC Evidence={ECO:0000269|PubMed:15569691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexanoyl-CoA + NAD(+) = (2E)-hexenoyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:52576, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:15569691};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:52578;
CC Evidence={ECO:0000269|PubMed:15569691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2E)-enoyl-CoA + H(+) + NADPH = a 2,3-saturated acyl-CoA +
CC NADP(+); Xref=Rhea:RHEA:33763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.38;
CC Evidence={ECO:0000269|PubMed:15569691, ECO:0000269|PubMed:30650145};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33764;
CC Evidence={ECO:0000269|PubMed:15569691, ECO:0000269|PubMed:30650145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + NADP(+) = (2E)-butenoyl-CoA + H(+) + NADPH;
CC Xref=Rhea:RHEA:27906, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.86;
CC Evidence={ECO:0000269|PubMed:15569691, ECO:0000269|PubMed:30650145};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27908;
CC Evidence={ECO:0000269|PubMed:15569691, ECO:0000269|PubMed:30650145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-hexenoyl-CoA + H(+) + NADPH = hexanoyl-CoA + NADP(+);
CC Xref=Rhea:RHEA:44956, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000269|PubMed:15569691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44957;
CC Evidence={ECO:0000269|PubMed:15569691};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=68 uM for (2E)-butenoyl-CoA (crotonyl-CoA) (in the presence of
CC NADH) {ECO:0000269|PubMed:15569691};
CC KM=91 uM for trans-2-hexenoyl-CoA (in the presence of NADH)
CC {ECO:0000269|PubMed:15569691};
CC KM=109 uM for NADH (in the presence of (2E)-butenoyl-CoA (crotonyl-
CC CoA)) {ECO:0000269|PubMed:15569691};
CC KM=119 uM for NADPH (in the presence of (2E)-butenoyl-CoA (crotonyl-
CC CoA)) {ECO:0000269|PubMed:15569691};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:15569691, ECO:0000305|PubMed:30650145}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15569691}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15569691,
CC ECO:0000269|PubMed:30650145}.
CC -!- DEVELOPMENTAL STAGE: Expressed under aerobic and anaerobic conditions.
CC {ECO:0000269|PubMed:15569691}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:15569691}.
CC -!- DISRUPTION PHENOTYPE: Severe bleaching phenotype concomitant with
CC negligible levels of chlorophylls and glycolipids. The levels of
CC alanine, glycine, tryptophan, and arginine, as well as those for
CC glycerophospholipids were highly impacted in the mutant under anaerobic
CC conditions. {ECO:0000269|PubMed:30650145}.
CC -!- MISCELLANEOUS: Euglena gracilis exhibits the metabolic behavior of a
CC plant in the light and of an animal in the dark.
CC {ECO:0000250|UniProtKB:Q9SWQ9}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000305}.
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DR EMBL; AY741582; AAW66853.1; -; mRNA.
DR AlphaFoldDB; Q5EU90; -.
DR SMR; Q5EU90; -.
DR SwissLipids; SLP:000001707; -.
DR KEGG; ag:AAW66853; -.
DR BioCyc; MetaCyc:MON-16778; -.
DR BRENDA; 1.3.1.44; 2197.
DR SABIO-RK; Q5EU90; -.
DR UniPathway; UPA00199; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IEA:RHEA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR HAMAP; MF_01838; FabV_reductase; 1.
DR InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR PANTHER; PTHR37480; PTHR37480; 1.
DR Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR Pfam; PF12241; Enoyl_reductase; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Mitochondrion; NAD; NADP; Oxidoreductase;
KW Transit peptide.
FT TRANSIT 1..68
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 69..539
FT /note="Trans-2-enoyl-CoA reductase"
FT /id="PRO_0000033619"
FT ACT_SITE 377
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q97LU2"
FT BINDING 190..195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q97LU2"
FT BINDING 216..217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q97LU2"
FT BINDING 253..254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q97LU2"
FT BINDING 281..282
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q97LU2"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97LU2"
FT BINDING 386
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q97LU2"
FT BINDING 412..414
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q97LU2"
SQ SEQUENCE 539 AA; 57303 MW; A52C244AC61E2CDF CRC64;
MSCPASPSAA VVSAGALCLC VATVLLATGS NPTALSTAST RSPTSLVRGV DRGLMRPTTA
AALTTMREVP QMAEGFSGEA TSAWAAAGPQ WAAPLVAAAS SALALWWWAA RRSVRRPLAA
LAELPTAVTH LAPPMAMFTT TAKVIQPKIR GFICTTTHPI GCEKRVQEEI AYARAHPPTS
PGPKRVLVIG CSTGYGLSTR ITAAFGYQAA TLGVFLAGPP TKGRPAAAGW YNTVAFEKAA
LEAGLYARSL NGDAFDSTTK ARTVEAIKRD LGTVDLVVYS IAAPKRTDPA TGVLHKACLK
PIGATYTNRT VNTDKAEVTD VSIEPASPEE IADTVKVMGG EDWELWIQAL SEAGVLAEGA
KTVAYSYIGP EMTWPVYWSG TIGEAKKDVE KAAKRITQQY GCPAYPVVAK ALVTQASSAI
PVVPLYICLL YRVMKEKGTH EGCIEQMVRL LTTKLYPENG APIVDEAGRV RVDDWEMAED
VQQAVKDLWS QVSTANLKDI SDFAGYQTEF LRLFGFGIDG VDYDQPVDVE ADLPSAAQQ
