ID   A0A0G1X4I5_9BACT        Unreviewed;       339 AA.
AC   A0A0G1X4I5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:KKU89330.1};
GN   ORFNames=UY19_C0016G0016 {ECO:0000313|EMBL:KKU89330.1};
OS   Candidatus Wolfebacteria bacterium GW2011_GWA2_47_9b.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1619005 {ECO:0000313|EMBL:KKU89330.1, ECO:0000313|Proteomes:UP000033882};
RN   [1] {ECO:0000313|EMBL:KKU89330.1, ECO:0000313|Proteomes:UP000033882}
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:KKU89330.1}.
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DR   EMBL; LCPB01000016; KKU89330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1X4I5; -.
DR   PATRIC; fig|1619005.3.peg.897; -.
DR   Proteomes; UP000033882; 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   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; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR   PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          8..328
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          106..303
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   339 AA;  37021 MW;  8A271AA35485E7D0 CRC64;
     MKIAFFQIED WEIEHIKEQL AGHELFFSKE KLSAEALPEQ RDFDIVSVFV GSKIDQAVLA
     ALPNLKLVTT RSTGFDHVDL PMAQSMNIAT GYVPGYGDNT VAEFAFGLIL ALSRKIYDSV
     DRLRETGVYS YVGLRGFDLQ GKTIGVMGTG RIGQHVIRIA KGFGMQVIAF DAFPKAELAT
     ELGFEYVGLD DLLGRSDVIT IHVPYLPSTH HLINMDSLTK IKKGALLINT ARGAVVETDA
     LVKGLADGIL GGAGLDVLEE EGVLADEKTL VLYGHPEEHN LKTVLENHVL IDMPNVLVTP
     HNAFNTQEAL QRILDTDICN IQEFLGKGIA KCPIPAPKA
//