ID   A0A0G0B8B8_9BACT        Unreviewed;       323 AA.
AC   A0A0G0B8B8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=D-glycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UR64_C0023G0008 {ECO:0000313|EMBL:KKP65613.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWE1_35_16.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618761 {ECO:0000313|EMBL:KKP65613.1, ECO:0000313|Proteomes:UP000034952};
RN   [1] {ECO:0000313|EMBL:KKP65613.1, ECO:0000313|Proteomes:UP000034952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       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:KKP65613.1}.
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DR   EMBL; LBPY01000023; KKP65613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0B8B8; -.
DR   PATRIC; fig|1618761.3.peg.792; -.
DR   Proteomes; UP000034952; 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; cd05301; GDH; 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; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          5..321
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..290
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   323 AA;  35268 MW;  651D14F10B177521 CRC64;
     MPKQIYITRE IPEAGLKLLR EKGIEFDMGT NDLPPSKKEI IKILKKKPYD GVISFLTDTI
     DEEIFNACPT ARIFANYSVG FNNIDLEVAK KRKVEISNTP GTSNIAVAEH TVALMLALTT
     RLVEGDRYMR AGKYKGWNPK LLMGTDMKGK TIGLVGGGAI GGEVAKILYK GFGSNIIYCD
     VVNNKKLEEE SGAVKKEFGD LMKTADIVSL HCPLLPSTTH LINKEALLMM KPTAFLINTA
     RGPIVDEYAL VLALKNKVIS GAALDVFEFE PKLAKGLSKL NNVILTPHIA SARETARNMM
     AEIAVKNIIS VFETGKAINS VLG
//