ID A0A0G0V9B5_9BACT Unreviewed; 328 AA.
AC A0A0G0V9B5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:KKR97583.1};
GN ORFNames=UU48_C0012G0022 {ECO:0000313|EMBL:KKR97583.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWF2_41_16.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618997 {ECO:0000313|EMBL:KKR97583.1, ECO:0000313|Proteomes:UP000034746};
RN [1] {ECO:0000313|EMBL:KKR97583.1, ECO:0000313|Proteomes:UP000034746}
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:KKR97583.1}.
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DR EMBL; LCAU01000012; KKR97583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0V9B5; -.
DR PATRIC; fig|1618997.3.peg.931; -.
DR Proteomes; UP000034746; 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 GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR029752; D-isomer_DH_CS1.
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; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 4..327
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 36444 MW; 714F21D65AD81D1F CRC64;
MTRIFITRAI PESGLKLLKK RKGLKIEVYE KDQIIPHREL LRRVKGVNIL LSLLTDRIDT
DIFDAAGPQL KLVANYAVGF DNIDVVEAKK RGIALTNTPG DEIAETVAEH TVAMMFALAH
RIVESDTFMR AGKYKGWNPN LFLGTDIIGK TLGIIGTGKI GTCLIRRVAE GFGIRILYHD
VRANPELEKT FHAVYRTKDQ LLKEADFVSL HVPLLPSTHH LIGTKELKRM KKTAFLINTS
RGPVIDIHAL VQALKTKQIA GAGLDVHECE PNIACNKEDI LTLRRLSNVI LTPHTASATI
ETRDAMSCRA AKNILAFLRG DIPPNLIK
//
