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Database: UniProt
Entry: A0A0G0X4D8_9BACT
LinkDB: A0A0G0X4D8_9BACT
Original site: A0A0G0X4D8_9BACT 
ID   A0A0G0X4D8_9BACT        Unreviewed;       335 AA.
AC   A0A0G0X4D8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UU29_C0012G0015 {ECO:0000313|EMBL:KKR82477.1};
OS   Candidatus Daviesbacteria bacterium GW2011_GWA2_40_9.
OC   Bacteria; Candidatus Daviesbacteria.
OX   NCBI_TaxID=1618424 {ECO:0000313|EMBL:KKR82477.1, ECO:0000313|Proteomes:UP000034601};
RN   [1] {ECO:0000313|EMBL:KKR82477.1, ECO:0000313|Proteomes:UP000034601}
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:KKR82477.1}.
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DR   EMBL; LCAB01000012; KKR82477.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0X4D8; -.
DR   PATRIC; fig|1618424.3.peg.927; -.
DR   Proteomes; UP000034601; 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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          14..334
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          107..304
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   COILED          255..282
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   335 AA;  37710 MW;  2DE94723B4C0005E CRC64;
     MKIGFFEITE TEKKDYFIQN LPGYELIFID KPLTEESLPQ ILDFDIISVF VNCQVTPKVI
     TAFPRLRLIT TRSTGFDNID LPFAKSKNIM VANVPAYGSH TVAEYTFGLM LALSRKIYQA
     AYRVKVGEDF TLQGLRGFDL CSKTLGVIGT GKIGSNVVSI AQGFNMKVLA FDAFPNEELA
     RTHNFLYTSL EELLKTADVV TLHTPYNEQT HHLINRQNIF LMKKGSLLIN TARGQVVETE
     ALFQALIQNH LGGAALDVLE EEKELKDEME VLAKNTQSAE ELKTILHNHI LINLPQVIIT
     PHMAFYSKEA EFAILETTEE NIKSFLQGNP KNIVH
//
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