ID B6H5M8_PENRW Unreviewed; 405 AA.
AC B6H5M8;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=enoyl-[acyl-carrier-protein] reductase {ECO:0000256|ARBA:ARBA00038963};
DE EC=1.3.1.104 {ECO:0000256|ARBA:ARBA00038963};
GN ORFNames=Pc14g00670 {ECO:0000313|EMBL:CAP74208.1}, PCH_Pc14g00670
GN {ECO:0000313|EMBL:CAP74208.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP74208.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP74208.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920429; CAP74208.1; -; Genomic_DNA.
DR RefSeq; XP_002560061.1; XM_002560015.1.
DR AlphaFoldDB; B6H5M8; -.
DR STRING; 500485.B6H5M8; -.
DR GeneID; 8310303; -.
DR KEGG; pcs:Pc14g00670; -.
DR VEuPathDB; FungiDB:PCH_Pc14g00670; -.
DR eggNOG; KOG0025; Eukaryota.
DR HOGENOM; CLU_026673_17_0_1; -.
DR OMA; YGYTQSK; -.
DR OrthoDB; 6213at2759; -.
DR BioCyc; PCHR:PC14G00670-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c14.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:UP000000724};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 55..399
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 405 AA; 44611 MW; B8511F79D2A1D0A4 CRC64;
MFSRSVLQTA TRSVRPASAR AVPQLGKAPF GRRYVSVYGY TQAKALIYSK YGEPKDVLRL
HKHSISAPHA TQVNLRLLTA PMNPADVNQI QGVYPSKPPF QTELGNVEPA AVGGNEGAFE
VLSTGAGVKN LSKGDWVIMK RTGLGTWRTH AQLDESQLIK VENKEGLTPL QVGTVSVNPV
TAYRMLRDFC EWDWMRAGEE WVIQNGANSG VGRAAIQLGR EWGIKTLNVI RQRKTPEETE
ALKQELRDLG ATVVITEEEM LNGNFRDMVH EFTRKGREPI RLALNCVGGK NATALAKTLA
PDSHMVTYGA MSKQPVALPS GLLIFKNLAF DGFWVSKWGD KNPQLKESTI KDVLQLTRSG
KFKDIPVDEV KWNWETEGPE LAESVQGTLG GYRSGKGVFT FSGGD
//
