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Database: UniProt
Entry: A0A428STM5_9HYPO
LinkDB: A0A428STM5_9HYPO
Original site: A0A428STM5_9HYPO 
ID   A0A428STM5_9HYPO        Unreviewed;       349 AA.
AC   A0A428STM5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Glycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CEP52_013454 {ECO:0000313|EMBL:RSL93113.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL93113.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSL93113.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL93113.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:RSL93113.1}.
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DR   EMBL; NKCK01000190; RSL93113.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428STM5; -.
DR   STRING; 1325735.A0A428STM5; -.
DR   Proteomes; UP000287144; 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   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:UP000287144}.
FT   DOMAIN          36..316
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          115..305
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   349 AA;  38076 MW;  3C9E23DF04A18D9D CRC64;
     MSRPATATEI PHHIVFLEAA NAPLPKFAFP HTYRRHPSTQ PHEIPERIKD ATIVILGGFA
     PITPEHLEHA PKLQCVAITA TGFDWLDRQA FAERGISVVN CPQNNVDAVG EHFLALYFAA
     RRKIVEVHNT VTAPERYWVK EGSLTPRWKQ GAPLSCHQEV LGIIGYGSLG RKVESLARGV
     GFGRILIAER KGESKVRDGR VHFELLLKTA TTIAVCCPKE PGTLGLISAP EFEMMKPEAL
     LLNISRGGIV CESALASALK QGTIFGAATD VLETEPGGIG TTPLIPDVAK GEEPVPNLTV
     TSHIAWFSQK TVENLDRMLR LGIEGFVKDT LLEQASRATV IVHKGEVFK
//
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