ID A0A0G1YIR1_9BACT Unreviewed; 334 AA.
AC A0A0G1YIR1;
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:KKW43328.1};
GN ORFNames=UY93_C0003G0111 {ECO:0000313|EMBL:KKW43328.1};
OS Parcubacteria group bacterium GW2011_GWA1_56_13.
OC Bacteria.
OX NCBI_TaxID=1618803 {ECO:0000313|EMBL:KKW43328.1, ECO:0000313|Proteomes:UP000034801};
RN [1] {ECO:0000313|EMBL:KKW43328.1, ECO:0000313|Proteomes:UP000034801}
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:KKW43328.1}.
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DR EMBL; LCRY01000003; KKW43328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1YIR1; -.
DR STRING; 1618803.UY93_C0003G0111; -.
DR PATRIC; fig|1618803.3.peg.701; -.
DR Proteomes; UP000034801; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 41..333
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 334 AA; 36740 MW; AB9CF217B4B7F7BC CRC64;
MKIRYFSGEL WEESYVRAKL PNEDIFFHAG PLATFKDLSD ADTEVLCTFI ESRIGADELK
RFPGLKLIAT RSTGFDHIDL KAAAARGVVV ANVPYYGEHT VAEFAFALLL ALSRRVIDAD
ERVRETGTFS HDNLRGFDLA GKTIGIVGCG HIGIHAIRMA NGFGMNVLGF DVRRDDELAR
THAFSYAELP ELLAASDIVS LHVPYNKHTH HLINRENVDF LKKGAYLINT SRGAVVETQA
LIDALQNGTL AGAGLDVLEE EGTLSDETAL LTAPHPNKEG LKLALENHYL IRHPRVIVTP
HTAFNTTEAV ERILDATVDN IRKFEAGSPT NIVS
//
