ID   A0A0G0KYC1_9BACT        Unreviewed;       307 AA.
AC   A0A0G0KYC1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:KKQ80605.1};
GN   ORFNames=UT02_C0005G0016 {ECO:0000313|EMBL:KKQ80605.1};
OS   Parcubacteria group bacterium GW2011_GWC2_38_7.
OC   Bacteria.
OX   NCBI_TaxID=1618920 {ECO:0000313|EMBL:KKQ80605.1, ECO:0000313|Proteomes:UP000034580};
RN   [1] {ECO:0000313|EMBL:KKQ80605.1, ECO:0000313|Proteomes:UP000034580}
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:KKQ80605.1}.
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DR   EMBL; LBVF01000005; KKQ80605.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0KYC1; -.
DR   STRING; 1618920.UT02_C0005G0016; -.
DR   Proteomes; UP000034580; 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          62..307
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          116..254
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   307 AA;  34403 MW;  E118F50BF7CB5791 CRC64;
     MKIILACPKK CFNEEEISTL QQFATEFIES KSINLDEVES LYSSDEFILV VDPTYLKESW
     DALPVERIEK MKGLKALCLT TSSFSWVDGK KLAEMGVILT NTPGKSTNAV AEFNIYMMMT
     LLRKIPLIAK NNWEMDYDNF INDEAKGKTA GVIGLGQIGS RVAELCAGLG LKVCYWDRKT
     KEVNYERMEL ADLLKKADVI FNTLATPPEV KGIITDEMIK SMKSTALIIS TSDPIYNQEF
     ILQQVAENKL GGFAFESDSK KFTDYKGNVM VFPEQAYLTN ETLANTSRIT TETILSVIKG
     TPINKVN
//