ETR1_SCHPO
ID ETR1_SCHPO Reviewed; 372 AA.
AC Q10488;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase, mitochondrial {ECO:0000250|UniProtKB:Q8WZM3};
DE EC=1.3.1.104 {ECO:0000250|UniProtKB:Q8WZM3};
DE AltName: Full=2-enoyl thioester reductase {ECO:0000250|UniProtKB:Q8WZM3};
DE Flags: Precursor;
GN Name=etr1; ORFNames=SPAC26F1.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA97361.1; -; Genomic_DNA.
DR PIR; T38416; T38416.
DR RefSeq; NP_594891.1; NM_001020320.2.
DR AlphaFoldDB; Q10488; -.
DR SMR; Q10488; -.
DR BioGRID; 278576; 2.
DR STRING; 4896.SPAC26F1.04c.1; -.
DR iPTMnet; Q10488; -.
DR MaxQB; Q10488; -.
DR PaxDb; Q10488; -.
DR PRIDE; Q10488; -.
DR EnsemblFungi; SPAC26F1.04c.1; SPAC26F1.04c.1:pep; SPAC26F1.04c.
DR GeneID; 2542100; -.
DR KEGG; spo:SPAC26F1.04c; -.
DR PomBase; SPAC26F1.04c; etr1.
DR VEuPathDB; FungiDB:SPAC26F1.04c; -.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_0_1; -.
DR InParanoid; Q10488; -.
DR OMA; HQLCRAW; -.
DR PhylomeDB; Q10488; -.
DR Reactome; R-SPO-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR PRO; PR:Q10488; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; ISO:PomBase.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISO:PomBase.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
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..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..372
FT /note="Enoyl-[acyl-carrier-protein] reductase,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000000903"
FT ACT_SITE 72
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 157
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 183..186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 206..208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 279..282
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 304..306
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 365
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
SQ SEQUENCE 372 AA; 41230 MW; F0ECE4624829A428 CRC64;
MSFFKTAVRR FSSTSITRGM AKAIAYSEYG NPKEVLRAVS YNVPKCSKNQ VNVRFLASPI
NPSDINQIQG VYPSKPPFTN DVCSSKPSAV AGNEGLVEVV DVGDQFKGTF SPGQWAILGS
VNLGSWRTEM NIDGRSLVPV DKSAFPSIAE AATLSVNPCT AYCLLQHVVQ LNKGDWFIQD
GANSMVGIAT IQLAKHFGYK SINVVRNRPD IEKLKEQLKS LGATIVITDE ELMDRKTMKQ
KVPEWIQGGE VKLGIDCVSG RVAAEMAKYM SKGATMATFG GMSRQPLPVP VSLLIFKNLK
FHGFWVTKWK SEHPEEFLKI IHKVEDFYRN GTLKTVNTEL VSLKEDADEK TFLDTFLNAI
EGHGKKIIKF EH
