ID F9X1Z7_ZYMTI Unreviewed; 393 AA.
AC F9X1Z7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=enoyl-[acyl-carrier-protein] reductase {ECO:0000256|ARBA:ARBA00038963};
DE EC=1.3.1.104 {ECO:0000256|ARBA:ARBA00038963};
GN ORFNames=MYCGRDRAFT_84372 {ECO:0000313|EMBL:EGP89684.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP89684.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP89684.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|ARBA:ARBA00010371}.
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DR EMBL; CM001197; EGP89684.1; -; Genomic_DNA.
DR RefSeq; XP_003854708.1; XM_003854660.1.
DR AlphaFoldDB; F9X1Z7; -.
DR STRING; 336722.F9X1Z7; -.
DR EnsemblFungi; Mycgr3T84372; Mycgr3P84372; Mycgr3G84372.
DR GeneID; 13395877; -.
DR KEGG; ztr:MYCGRDRAFT_84372; -.
DR VEuPathDB; FungiDB:ZTRI_2.45; -.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_0_1; -.
DR InParanoid; F9X1Z7; -.
DR OMA; YGYTQSK; -.
DR OrthoDB; 6213at2759; -.
DR Proteomes; UP000008062; Chromosome 2.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:EnsemblFungi.
DR GO; GO:0009060; P:aerobic respiration; IEA:EnsemblFungi.
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; 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; 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:UP000008062};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 50..390
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 393 AA; 42846 MW; 2849F79D6E27F62A CRC64;
MASSWNLLTA TPRTLLRSAP KVLPSSRRSI SAYGYEQAKC LILPNTGEPK DVLRLHSHSI
SPPTGNLVTL QLLASPINPA DINQIQGVYP TPPTWTTSLG TPDKIAVGGN EGVAKVIAKG
GNVKGVQKGD WVIFKKQGFG TWRTHAQTDV SNVTVVKNTD GLKPEQVGTV SVNPCTAWRM
LKDFGTVKEG EWFVQNGANS GVGRAAIQLG KLWGMRSINV VRKRETGHEE LVKELEGLGA
DVVVTEEELN GKEFKDRVKE LTNGGREPVR LGLNCVGGKL VNSMAKLLAP GSAMVTYGAM
SKQPVTLPMG LLIFKDIQFK GFWVSRWSDA NPEEKMKCVE EVMDLTKKGR FKDVPMQTVK
WDRGTKQEEL VDAVQGTLDG YRSGKGIFVF GET
//
