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
//