ID   A0A0G0I397_9BACT        Unreviewed;       317 AA.
AC   A0A0G0I397;
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=Uncharacterized protein {ECO:0000313|EMBL:KKQ18729.1};
GN   ORFNames=US31_C0002G0074 {ECO:0000313|EMBL:KKQ18729.1};
OS   Berkelbacteria bacterium GW2011_GWA1_36_9.
OC   Bacteria; Candidatus Berkelbacteria.
OX   NCBI_TaxID=1618331 {ECO:0000313|EMBL:KKQ18729.1, ECO:0000313|Proteomes:UP000034508};
RN   [1] {ECO:0000313|EMBL:KKQ18729.1, ECO:0000313|Proteomes:UP000034508}
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|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:KKQ18729.1}.
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DR   EMBL; LBSM01000002; KKQ18729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0I397; -.
DR   Proteomes; UP000034508; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          34..317
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          113..285
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   317 AA;  35699 MW;  2C2200D7B81D3333 CRC64;
     MNKKFKKILT IGIDKSALDS AYWQRIETLA EKIINLVKDS SEIKEQLVNT DCLLIGFGVI
     INKEIIDNAP KLKYIGVLAT AYGKVDVDYA KSKEIAVCNI PGYATEAVAE FVFAVILDHI
     RETGRGKKQA RGGNYSEVGF LAVEIKNKIF GILGLGRIGS RVAEIALGFG ADVRYWNMGR
     KKDFEISRVK YEEADKLIPK CDFLSLHFAQ VKDTENFLNE ERIQKIKKGA VVINTAPMEL
     VNIDALEKRL KNRDITFILD HSDEMSPENI KRLSKFENCI IYPPIAYITK EARIAKQEIF
     VGNIGNFLKE SSTNQVN
//