ID G3XM58_ASPNA Unreviewed; 425 AA.
AC G3XM58;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=ASPNIDRAFT_54418 {ECO:0000313|EMBL:EHA28171.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA28171.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA28171.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHA28171.1}.
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DR EMBL; ACJE01000001; EHA28171.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XM58; -.
DR STRING; 380704.G3XM58; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1155665; -.
DR HOGENOM; CLU_026673_16_2_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR CDD; cd08249; enoyl_reductase_like; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR PANTHER; PTHR43482; PROTEIN AST1-RELATED; 1.
DR PANTHER; PTHR43482:SF2; ZINC-BINDING DEHYDROGENASE FAMILY, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15030)-RELATED; 1.
DR Pfam; PF08240; ADH_N; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 62..421
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 425 AA; 46341 MW; 51DD081EBA525D8F CRC64;
MTTISTYTLP APVEEKYTAV YHREFVLEQR TDPTYTSTPS APTESIIPPK TTQRALLLHA
AGEQYTLVTD HAIPEISHKD EILVKIQAVG LNPVDWKGPA FNFGLPSLPW INGRDLAGEV
VRVNNENSRV RVGDKVLVPS TDYRDIRKAA FQEYAVATHF NAARIPSNSC VHASASLGVA
FVASVLALGV SLGLDFRQCL QCPGPNLQDT VTQLDINNIP ADIRGECFSS SAVPERLSKG
EWIAIWGAST TTGYITLQLA KLAGLRVICV ADIARHGLRL HQLGADVLVD RQDTERAVDI
IRGVTGGKLR YAVDIVGAET ATLLQRTLDD TIREDGSHSH LLGLTGLPKE RNEALVYHTV
PIKLFHTSPT VGEQMVSWLE ALLETEALQL PEVVRHEGGL GSINESLEVL RKGSVSGKRI
VVDME
//
