ID A0A395T0S9_9HYPO Unreviewed; 314 AA.
AC A0A395T0S9;
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=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0000259|Pfam:PF02826};
GN ORFNames=FLONG3_3916 {ECO:0000313|EMBL:RGP77959.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP77959.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP77959.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP77959.1,
RC ECO:0000313|Proteomes:UP000266234};
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 -!- 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:RGP77959.1}.
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DR EMBL; PXOG01000081; RGP77959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395T0S9; -.
DR STRING; 694270.A0A395T0S9; -.
DR Proteomes; UP000266234; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12160; 2-Hacid_dh_3; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234}.
FT DOMAIN 103..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 314 AA; 34492 MW; 5EF5153D9A26DDC6 CRC64;
MKLLYPTSLE LDIKSLEGFS VDLHPYDVKK PIPEEHVDAE VLVTWTNTAE NLKDAAKRLT
KLQWIQSLAA GPNDVLNAGF DASKIKITTG SGLHDHTVAE HALGLLLNAA RRFYEMRDYQ
LQGKWPGHLG GPQPDRPKDK FTTLRDARVL IWGFGNIAKN LTPLLVGLGA QVRGIARQKG
VRNGIEIYTE DDLDKLLPET DALVMILPGS DSTRHVLNAE RLKQLPKHAW VVNVGRGTSV
DEDALVDALE KGEIGGAALD VFETEPLPEP SKIWKAPNTI VSPHAAGGRP QGAEALIADN
LRRFRATQDL KNII
//
