ID A0A319DEZ5_9EURO Unreviewed; 407 AA.
AC A0A319DEZ5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:PYH89633.1};
GN ORFNames=BO71DRAFT_444450 {ECO:0000313|EMBL:PYH89633.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH89633.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH89633.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH89633.1,
RC ECO:0000313|Proteomes:UP000247810};
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|ARBA:ARBA00001947,
CC 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; KZ826020; PYH89633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DEZ5; -.
DR STRING; 1448320.A0A319DEZ5; -.
DR Proteomes; UP000247810; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF2; PKS_ER DOMAIN-CONTAINING PROTEIN-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:UP000247810};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 40..404
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 407 AA; 43591 MW; D642E89EE52F15C8 CRC64;
MSQSHPDSIS ACRLNNEFTY TPWITHSLPP AAHLSPMART RPGGWKLQNV ALRSLREHEL
VVEVVASGVC QTDLHFGGLE SGHGVHYPRV MGHEGAGYVR EIGPGVTTAR VGDPVLMSFS
SCQSCRCCRR GHPAHCEIFD PINFESTAEN RVFWAEKEEG STHGAEPDIF GQFFGQSTFA
SRTVVQETAV VNVAGLVESR EQLQLLAPLG CGIQTGAGAV LHAANTQRED TVAVLGLGGV
GLSAVMGARI AGCKTIIGIA RNKARLKLAL ELGATHVVRI DPDADISLVT DDVRALTGGL
GVDVTLETTG VPELVAEGIR MTANKGRIVQ LGTAPENASL SLPIHEFMVA GKTYIGVVEG
DVIPREFVPK MIEWVRTMDN FVHITADGKL AFLIIVVSYL RPGHDPN
//
