ID A0A0G1QY59_9BACT Unreviewed; 326 AA.
AC A0A0G1QY59;
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:KKU49906.1};
GN ORFNames=UX71_C0004G0013 {ECO:0000313|EMBL:KKU49906.1};
OS Parcubacteria group bacterium GW2011_GWA1_47_10.
OC Bacteria.
OX NCBI_TaxID=1618791 {ECO:0000313|EMBL:KKU49906.1, ECO:0000313|Proteomes:UP000033978};
RN [1] {ECO:0000313|EMBL:KKU49906.1, ECO:0000313|Proteomes:UP000033978}
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:KKU49906.1}.
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DR EMBL; LCNF01000004; KKU49906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1QY59; -.
DR Proteomes; UP000033978; 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 5..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 35496 MW; 5D4BFC2A31FD343B CRC64;
MTKVIFVTRK IPEIGIQKLR DKGYEVDVNE SESIPTQDQL LGFLKTKPYD AVITLLTDKI
DSKIFDATPS VKLYANYATG FDNIDVAEAG RRGIMVANAP AELTSEAVAE HTIALMLALA
ARIVESDEYV RKGLYQGWSP MNFIGTDVLG KTLGIVGAGR IGGRVGKYAR GLGMKIVYTD
VARNEKFEAE CGAVYKSSLE EVLSEADIVS LHVPLFESTR HLMNKESFSK MKPTSFLINT
SRGPVVEESA LEEALKTGVI AGAALDVFEF EPKISDGLIK LQNIILTPHI ASASIEARNQ
MAELAADNVI DFLEGATPRN LVNPMP
//
