ID A0A0G0T2L0_9BACT Unreviewed; 335 AA.
AC A0A0G0T2L0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:KKR71278.1};
GN ORFNames=UU12_C0004G0025 {ECO:0000313|EMBL:KKR71278.1};
OS Candidatus Woesebacteria bacterium GW2011_GWA2_40_7b.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618563 {ECO:0000313|EMBL:KKR71278.1, ECO:0000313|Proteomes:UP000034562};
RN [1] {ECO:0000313|EMBL:KKR71278.1, ECO:0000313|Proteomes:UP000034562}
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:KKR71278.1}.
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DR EMBL; LBZK01000004; KKR71278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0T2L0; -.
DR STRING; 1618563.UU12_C0004G0025; -.
DR PATRIC; fig|1618563.3.peg.111; -.
DR Proteomes; UP000034562; 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 CDD; cd05301; GDH; 1.
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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 5..325
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 335 AA; 37169 MW; 0DF3A315568CE030 CRC64;
MRIFVTRKIP GDHLEKLKVD GNEVAISEFD RPLTQEELLD RGKGADILLT LLTDRIDGDL
MDAIGPQLKM ISNYAVGFDN VDIKAATDRQ IVVTNTPSTE VNEAVAEHTW VFIMALARRV
VEADEFVRQE GYFTEKGGYK GWEPNLFLGQ SILGKTLGII GLGRIGSMVA KRAKGYNMTV
LYNKSKPDSE AEAELGVKFV TLDELYKQSD FLTLHVPLTD QTRHMINENV FNKMKKGAFL
INTARGAVVD EKDLIDSLKS GKLGGVALDV FDNEPNISAE LIAAPNVILT PHIASATWEA
RNKMGEQAVK AILDVISDKK PENLVDEAVW NKRRK
//
