ID A0A3D8S4F5_9EURO Unreviewed; 351 AA.
AC A0A3D8S4F5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=DSM5745_04740 {ECO:0000313|EMBL:RDW81183.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW81183.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW81183.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW81183.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:RDW81183.1}.
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DR EMBL; PVWQ01000005; RDW81183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8S4F5; -.
DR STRING; 1810919.A0A3D8S4F5; -.
DR OrthoDB; 2084524at2759; -.
DR Proteomes; UP000256690; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd08234; threonine_DH_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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000256690};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..348
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 351 AA; 37927 MW; 9B6E0B31DB546101 CRC64;
MDAFNLPMKM KALEYSAPRN PRVVEKRLPN IRGHDLLIKV KACGVCGTDL HIHDGEFGAQ
FPVVPGHETV GVVAAYGSKV KGFSVGDRVV ADNSELCGEC FHCRRGSELF CENFIAHGVM
VDGGFAEYAV YPAKRVFPIQ SISDVDATLI EPAACAAHGI DKIAPQMGSR VLLFGAGPTG
LVLAQLLRQN GGCNVVVAAP EGAKMALARS LDAADEYICL PRDQAAAAAV LEKLEGGNPY
GFDIVVEATG NAKVLERALD FVRKGGKLVV YGVYGDDDRI SLPPNRIFKD EIQILGSFSE
MHKFPAAIDY LESGRVRVTG IVNQTFRVEQ WEECLEAMRT KKAIKAAIVF D
//
