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Database: UniProt
Entry: A0A428UAQ4_9HYPO
LinkDB: A0A428UAQ4_9HYPO
Original site: A0A428UAQ4_9HYPO 
ID   A0A428UAQ4_9HYPO        Unreviewed;       344 AA.
AC   A0A428UAQ4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=CEP52_003053 {ECO:0000313|EMBL:RSM11385.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM11385.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM11385.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM11385.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         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:RSM11385.1}.
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DR   EMBL; NKCK01000018; RSM11385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428UAQ4; -.
DR   STRING; 1325735.A0A428UAQ4; -.
DR   Proteomes; UP000287144; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08284; FDH_like_2; 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; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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|RuleBase:RU361277};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287144};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          1..342
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   344 AA;  36988 MW;  D13CAB1B5E77A84C CRC64;
     MSMRAVVFKG VGSPIPTIQD PRDAIIKVTV AALCGSDLHW YRGHQKIPVG FIPGHEFAGV
     IHELGSQVTG LNVGDSVVAT FTTQCGECFY CKRRQTSRCA RSFLFGNSAG TTSIDGGQAE
     YVRVPYSSST LVKRPKEIPE NMLVLMGDIF PTGYFAASRF LKNVPQEEAK SSTTVVVGCG
     PVGICAIAAA SSWCDNIIAI DMVPERLEEA RRLGATPILL SDDPVSKVLA ATDGRGADVV
     LEVVGNAAAM KLCVELVRPF GCISSVGVQT EELAFDGPSL YAKNVTIAWG RCPVRGIFEE
     ALACLSKVHD KLAFLCQCRM KLVEAPEAYE IFNARKVHKV LLSP
//
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