ID   A0A0G1KUD4_9BACT        Unreviewed;       311 AA.
AC   A0A0G1KUD4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:KKT87231.1};
GN   ORFNames=UW86_C0006G0006 {ECO:0000313|EMBL:KKT87231.1};
OS   Microgenomates group bacterium GW2011_GWA1_Microgenomates_45_10.
OC   Bacteria.
OX   NCBI_TaxID=1618493 {ECO:0000313|EMBL:KKT87231.1, ECO:0000313|Proteomes:UP000034781};
RN   [1] {ECO:0000313|EMBL:KKT87231.1, ECO:0000313|Proteomes:UP000034781}
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:KKT87231.1}.
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DR   EMBL; LCJY01000006; KKT87231.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1KUD4; -.
DR   Proteomes; UP000034781; 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   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 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          64..311
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          117..257
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   311 AA;  35321 MW;  562930BB68D53003 CRC64;
     MDNIQLIFLS PSFNEVVGDV LRQRLKSSGH LNVVTKPEDL DKVKQLFTKG NKVLAIDPLF
     CNWTVPNMLI SKITNLKAIC LMTRSADWVD ASFTRELGIP LTNTRDFYVE AVSEWAIMMM
     FCLARRIPLV AKSGWQQRYG KFQGVEVMGK TVGIIGMGQI GQRIAQQCQG LGMKVQYWSP
     HTHNDRYWYV SLNKLLATSD VVFPTYRLSA GERMLPGETK LNRLGRKAIL IDVVRIDNKD
     HEFLLRQVAK DKLFGYGFEE DGGNHFDKYK GNVWAGPALA WVTDRAMKLQ AESWVESVVQ
     ATKGNFPNRV N
//