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Database: UniProt
Entry: E3RNL6_PYRTT
LinkDB: E3RNL6_PYRTT
Original site: E3RNL6_PYRTT 
ID   E3RNL6_PYRTT            Unreviewed;       345 AA.
AC   E3RNL6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Glycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PTT_10171 {ECO:0000313|EMBL:EFQ92675.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ92675.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ92675.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; GL534220; EFQ92675.1; -; Genomic_DNA.
DR   RefSeq; XP_003299221.1; XM_003299173.1.
DR   AlphaFoldDB; E3RNL6; -.
DR   STRING; 861557.E3RNL6; -.
DR   EnsemblFungi; EFQ92675; EFQ92675; PTT_10171.
DR   KEGG; pte:PTT_10171; -.
DR   eggNOG; KOG0068; Eukaryota.
DR   HOGENOM; CLU_019796_1_3_1; -.
DR   OrthoDB; 1462550at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd05198; formate_dh_like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR   Pfam; PF00389; 2-Hacid_dh; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT   DOMAIN          31..342
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          136..314
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   345 AA;  37605 MW;  FB7F73F2C0984153 CRC64;
     MHHEIVALEG QHQPLPTAGF DFPAAVTYTL TTYESTRTRE ELLARIRNAT IVIATVVKID
     AEALDPSVTP NLRYIAVSAT GTDLIDLDAC RARGIRVTNC PGANLDAVSE HALSLYFAAR
     RRTVLLDRIT RTQPSEWRTK GTVNRYMRLP DGTPPITCKD EVMGVIGYGG LGKRIAALGQ
     ALGMRVLVAS RKTPAAPLQS DGLPAPNMAD DRIPFHDVLR QSTVVVLSLP RNSDTLNLIS
     TAELAKMHPY AVLINISRGG IVHEAAVVQA LKEKRIAGYA TDVYQVEPVG GPEDTPLLEE
     DTRDLNITMS PHLAWFSQRT VKNLGHLLKE TVEAWATGNP VNVIV
//
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