ETR2_DEBHA
ID ETR2_DEBHA Reviewed; 387 AA.
AC Q6BV30;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase 2, mitochondrial;
DE EC=1.3.1.104;
DE AltName: Full=2-enoyl thioester reductase 2;
DE Flags: Precursor;
GN Name=ETR2; OrderedLocusNames=DEHA2C05808g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of trans-2-enoyl
CC thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis
CC type II). Fatty acid chain elongation in mitochondria uses acyl carrier
CC protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP
CC and CoA thioesters as substrates in vitro. Required for respiration and
CC the maintenance of the mitochondrial compartment.
CC {ECO:0000250|UniProtKB:P38071}.
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:0000250|UniProtKB:P38071};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8WZM3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P38071}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; CR382135; CAG85995.1; -; Genomic_DNA.
DR RefSeq; XP_457939.1; XM_457939.1.
DR AlphaFoldDB; Q6BV30; -.
DR SMR; Q6BV30; -.
DR STRING; 4959.XP_457939.1; -.
DR EnsemblFungi; CAG85995; CAG85995; DEHA2C05808g.
DR GeneID; 2900740; -.
DR KEGG; dha:DEHA2C05808g; -.
DR VEuPathDB; FungiDB:DEHA2C05808g; -.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_0_1; -.
DR InParanoid; Q6BV30; -.
DR OMA; HQLCRAW; -.
DR OrthoDB; 1269870at2759; -.
DR Proteomes; UP000000599; Chromosome C.
DR GO; GO:0005759; C:mitochondrial matrix; 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 InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Mitochondrion; NADP; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..387
FT /note="Enoyl-[acyl-carrier-protein] reductase 2,
FT mitochondrial"
FT /id="PRO_0000000901"
FT ACT_SITE 79
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 199..202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 222..224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 297..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 322..324
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 382
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
SQ SEQUENCE 387 AA; 42554 MW; 800D3F11D4B64126 CRC64;
MYRNQLARAS LRSTSSINQI RNMITAQAVV YAQHGEPKDV LKTLKYEIDD DNLDSNSIIV
KTLGSPVNPS DINQIQGVYP SKPEKTTELG SNEPVAVCGN EGLFEILKVG DNVSNFKVGD
WCVPTSVNMG TWRTHMLCGG DEMTKIPNPE QSKANGKPSG LSVNQGATIS VNPLTAYLML
THYVKLTPGK DWFIQNGGNS AVGKYATQIS NLLGINSISV IRDRPDLQDL IKNMTEECGA
TKVITEEQNA SKEFGSEIKS WVKETGGEIK LALNCVGGKN STGIARKLNN NGLMLTYGGM
SMQPVILPTS LHIFKNITSS GFWVTQLLKN DVELKRKTLG QIIEWYENRQ LKDAPSKETK
FNPSDELSRY YIDGIVNSKG GKQLIVY
