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Database: UniProt
Entry: A0A395IA16_ASPHC
LinkDB: A0A395IA16_ASPHC
Original site: A0A395IA16_ASPHC 
ID   A0A395IA16_ASPHC        Unreviewed;       342 AA.
AC   A0A395IA16;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:RAL17100.1};
DE   Flags: Fragment;
GN   ORFNames=BO97DRAFT_360803 {ECO:0000313|EMBL:RAL17100.1};
OS   Aspergillus homomorphus (strain CBS 101889).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL17100.1, ECO:0000313|Proteomes:UP000248961};
RN   [1] {ECO:0000313|EMBL:RAL17100.1, ECO:0000313|Proteomes:UP000248961}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL17100.1,
RC   ECO:0000313|Proteomes:UP000248961};
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   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; KZ824268; RAL17100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395IA16; -.
DR   STRING; 1450537.A0A395IA16; -.
DR   VEuPathDB; FungiDB:BO97DRAFT_360803; -.
DR   OrthoDB; 1462550at2759; -.
DR   Proteomes; UP000248961; 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:UP000248961}.
FT   DOMAIN          34..341
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          116..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   NON_TER         342
FT                   /evidence="ECO:0000313|EMBL:RAL17100.1"
SQ   SEQUENCE   342 AA;  37442 MW;  5A8ACBF2FFA47B95 CRC64;
     MAQNSSTHHN IVFLQGDFVQ IPDFDLPAPH TYTKTIYSQT SLSEIHERIH DASVIVLSAL
     RIDASALAFE ISPNLKLVMV VAVGTDCIDL EACRKRGIVV SYIPAANTEA VSEHAIALHL
     ATRRKIMMMH ALTRAGEWPR RKTLMFDFVD KAGTPPLTCQ EEVAGIIGNG AVGKRIAHLA
     RGLGMKVIIS DRKQLGEAKT TNNSNDDLER IPFESVIRQS TVIFVAVPLM NTTRNLISTA
     EFEAMSPHAV LVNVSRGGVI DEDALVKALK EDRISGASTD VFFQEPASPD NSPLLAEGTE
     VLNLLVTPHL AWLAQKTMVN YSQRLKLSVE EWCKGSPLNV VT
//
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