ID A3LNF3_PICST Unreviewed; 366 AA.
AC A3LNF3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=enoyl-[acyl-carrier-protein] reductase {ECO:0000256|ARBA:ARBA00038963};
DE EC=1.3.1.104 {ECO:0000256|ARBA:ARBA00038963};
GN Name=ETR2 {ECO:0000313|EMBL:ABN64846.1};
GN ORFNames=PICST_34892 {ECO:0000313|EMBL:ABN64846.1};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN64846.1, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN64846.1, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC {ECO:0000256|ARBA:ARBA00010371}.
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DR EMBL; CP000496; ABN64846.1; -; Genomic_DNA.
DR RefSeq; XP_001382875.1; XM_001382838.1.
DR AlphaFoldDB; A3LNF3; -.
DR STRING; 322104.A3LNF3; -.
DR GeneID; 4836725; -.
DR KEGG; pic:PICST_34892; -.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_0_1; -.
DR InParanoid; A3LNF3; -.
DR OMA; YGYTQSK; -.
DR OrthoDB; 6213at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 17..355
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 366 AA; 39911 MW; C0064E4B22D1C4D3 CRC64;
MITAQAVVYS EHGEPKDVLR THTYEIDDDK IAANQIIVKT LGSPVNPSDI NQIQGVYPSK
PDKTTELGTS EPSAPCGNEG LFEIIKVGSN VSNFKVGDWA VPSNVNFGTW RTHALATEDQ
FTRLPNPEQS KAAGKPSGLT INQGATILVN PMTAYLMLTH YVQLIPGKDW FIQNGGNSAV
GKYAIQISKL LGFNSISVVR DRPNLNELES ELKGLGATQV ITEEQNGSRE FGPTIKNWVK
ETGGEIKLAL NCVGGKNSTG VARKLANNGL MLTYGGMSFQ PVILPTSLHI FKNITSAGFW
ITALLKNDEE LKNKTLSKIV EWYENEQLVD AKSLETPFVA GGAKQLHEYY QEAVVNSAKG
KQLITY
//