ID A0A0G1JAD9_9BACT Unreviewed; 328 AA.
AC A0A0G1JAD9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:KKT68245.1};
GN ORFNames=UW62_C0001G0009 {ECO:0000313|EMBL:KKT68245.1};
OS Candidatus Collierbacteria bacterium GW2011_GWB1_44_35.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1618383 {ECO:0000313|EMBL:KKT68245.1, ECO:0000313|Proteomes:UP000034604};
RN [1] {ECO:0000313|EMBL:KKT68245.1, ECO:0000313|Proteomes:UP000034604}
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|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:KKT68245.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCJA01000001; KKT68245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1JAD9; -.
DR PATRIC; fig|1618383.3.peg.9; -.
DR Proteomes; UP000034604; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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; 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 7..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 36293 MW; 6853EB4E862AEC79 CRC64;
MDKPKIFVTH KLPGKFSERL AKDYEVEVWP EKDISRTDLL EKVKGVTGII SLLTEKIDAE
VMDVAGNNLK VISNYAVGYD NIDVEAATKR GICVTNTPGV LTESVAEHVI GLAISLLKRI
SEGDRFVRSG KYHGWEPDLL VGTGLRDKVM GIAGLGRIGR WTARMSIALG MKVIYFNRHR
DEEFEEEYGV VYHTLEQLLE QSDVVSLSVP LTEETRHMIG ETQLKLMKKT AILINTARGP
IVDEEALIKS LNEKWIAGAG LDVFEDESGV PEALRSLPNT VLTPHIASAT IEARMAMARL
VVENLMDALA GRQPACLVNV SVWESKID
//
