ID A0A0M9GRV0_9BACI Unreviewed; 320 AA.
AC A0A0M9GRV0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KPB04283.1};
GN ORFNames=AAV98_12855 {ECO:0000313|EMBL:KPB04283.1};
OS Bacillus sp. CHD6a.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB04283.1, ECO:0000313|Proteomes:UP000037908};
RN [1] {ECO:0000313|EMBL:KPB04283.1, ECO:0000313|Proteomes:UP000037908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHD6a {ECO:0000313|EMBL:KPB04283.1,
RC ECO:0000313|Proteomes:UP000037908};
RA Lin W., Liu Y., Zheng Q., Jiao N.;
RT "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea
RT hydrothermal environment.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KPB04283.1}.
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DR EMBL; LBMD01000015; KPB04283.1; -; Genomic_DNA.
DR RefSeq; WP_060665972.1; NZ_LBMD01000015.1.
DR AlphaFoldDB; A0A0M9GRV0; -.
DR STRING; 1643452.AAV98_12855; -.
DR PATRIC; fig|1643452.3.peg.1426; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000037908; 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; cd05300; 2-Hacid_dh_1; 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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 7..310
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..280
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 320 AA; 36223 MW; 7C86051C535CEE23 CRC64;
MTKRLMLITQ NIGDAYTQQI KEMAPDFDLI IGKDKEIWAP HVKNAEIIVG WKKELDNLSL
TKGSPLKWIQ SWSAGVNSMP LSTLSEKGII LTSANGVHAY PISETIFALM LGLTRKVHTY
VKQQQEKVWH HAQMNLEIHE KTVGIIGVGE IGKETAKIAK AFRMNVLGVR HSGKPTDYVD
EMYTPDRLHE ILPKCDYVVI TLPLTEETEG MFGSEEFNRM KKSAFFINIG RGEVVVENDL
VQALQENDIA GAGLDVFIKE PLHENSPLWD MNNVIITPHT SGSTEHYSKR VIEDIFIPNL
KHYLKNEKPL INVVDYKKGY
//
