ID A0A395HLZ6_ASPHC Unreviewed; 374 AA.
AC A0A395HLZ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=GroES-like protein {ECO:0000313|EMBL:RAL08636.1};
GN ORFNames=BO97DRAFT_445978 {ECO:0000313|EMBL:RAL08636.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL08636.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL08636.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL08636.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KZ824311; RAL08636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HLZ6; -.
DR STRING; 1450537.A0A395HLZ6; -.
DR VEuPathDB; FungiDB:BO97DRAFT_445978; -.
DR OrthoDB; 5353053at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF3; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01980)-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.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 15..365
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 374 AA; 40361 MW; 0348C5E467C522DC CRC64;
MPAQPDQFHG WVSHSPTEPL TFTTFTAKPF EPTDLEIEIT HCGICGTDVH TLRSGWGPAD
YPCVVGHEIV GHITRLGAAV PSLPAPYSAF QIGDRVGVGA QILACLLPDC DACSTGQENY
CPRITGTYND RFYDATFLKK TAVKTMGGLA RTWRGPAQFV FKIPDALSSA HAAPLLCAGA
TVFTPLRKYG AGEGKRVGVV GIGGLGHLGV LFAKAMGCER VVAISRSSAK RQDVVEGLGA
DGFIATGEEE NWAKKYERTL DLIICTVDGD DMPLSRYLRL LRVGGTFVQV GAPEKPLPQV
LAWAFIQKGV SLAGSNIGSR EDIRAMLELA AQKNVLPWIE KRPMEEVNAA LKDMDAGRAR
YRYVLENGEP DSKL
//
