ID A0A1D8GAD0_9ACTN Unreviewed; 340 AA.
AC A0A1D8GAD0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:AOT62406.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:AOT62406.1};
GN ORFNames=A4G23_05302 {ECO:0000313|EMBL:AOT62406.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT62406.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT62406.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT62406.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-2016) 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; CP017316; AOT62406.1; -; Genomic_DNA.
DR RefSeq; WP_069979196.1; NZ_CP017316.1.
DR AlphaFoldDB; A0A1D8GAD0; -.
DR STRING; 285473.A4G23_05302; -.
DR KEGG; srn:A4G23_05302; -.
DR PATRIC; fig|285473.5.peg.5588; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000095349; Chromosome.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12167; 2-Hacid_dh_8; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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 ECO:0000313|EMBL:AOT62406.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095349}.
FT DOMAIN 48..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 124..300
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 340 AA; 36209 MW; 0BDDF4F719B300D6 CRC64;
MTPSAHRRPR TVLAMEPRVR DALFDAAARR RLTAVAATDP AVAVRDFTAP EHAAALAGAE
ALLTGWGCPP LTESALERMP RLRTVVHAAG SVKHHVTDAC WQRGITVASA AAANALPVAE
YTVAAVLFAG KRVLDAQRAY RERRGRVDAP ALLAGAGNFR RTVGVVGASR VGRRVIELLR
PYDLRVLLYD PYVTGEEAAR LGVRAVDLDE LARAGDVVTL HAPELPGTRH LFDRARLALM
PDGATLVNTA RGSLVDTEAL TRELVAGRLS AVLDVTEPEV PPAGSPLYDL PNVLLTPHVA
GSLGNELGRL AHTALDELER YGHGLPYAGP VRPGDLPRSA
//
