ID A0A395NXC9_TRIAR Unreviewed; 341 AA.
AC A0A395NXC9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=NAD-dependent epimerase/dehydratase domain-containing protein {ECO:0000259|Pfam:PF01370};
GN ORFNames=TARUN_2066 {ECO:0000313|EMBL:RFU80151.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU80151.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU80151.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU80151.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily.
CC {ECO:0000256|ARBA:ARBA00023445}.
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:RFU80151.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PXOA01000123; RFU80151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NXC9; -.
DR STRING; 490622.A0A395NXC9; -.
DR Proteomes; UP000266272; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10366:SF862; EPIMERASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266272}.
FT DOMAIN 6..213
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 341 AA; 36818 MW; F9E645331B0C1962 CRC64;
MAGDLVLLTG ATGFIGFRTL VLLLEAGYKV RTAVRNVAGF EKIKALKSAA PYVSQMEHIV
VTDITAPGAY DDAVKGVKYI VHVASPFASP DLLESEYESS YIQPAIKGST GILDSAAAIA
GIERVVITGS ILSIAGFGIN GTDAIVNETH RSAVTAGPYG SWIQAYAASK ALALEATKEW
MAEHKPPFDL ITIEPVFVLG RDETATTVDM LVKGANASLL GPLIGRQQPY PVPCNPVHVD
DVALMHVRSL DPTIPGNEDY LSNSHSLQNL QWDQSFDVIK KHYPKECAEG VFKIDTTPRP
KTLKLRIDST KAEKTFGITF KSFEEQILSA AGQYLELIGR K
//
