ID A0A196MNK6_9SPHN Unreviewed; 332 AA.
AC A0A196MNK6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:OAN56959.1};
GN ORFNames=A7Q26_17210 {ECO:0000313|EMBL:OAN56959.1};
OS Sphingobium sp. TCM1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=453246 {ECO:0000313|EMBL:OAN56959.1, ECO:0000313|Proteomes:UP000078322};
RN [1] {ECO:0000313|EMBL:OAN56959.1, ECO:0000313|Proteomes:UP000078322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCM1 {ECO:0000313|EMBL:OAN56959.1,
RC ECO:0000313|Proteomes:UP000078322};
RA Takahashi S.;
RT "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT Bacteria.";
RL Submitted (MAY-2016) 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:OAN56959.1}.
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DR EMBL; LXVX01000008; OAN56959.1; -; Genomic_DNA.
DR RefSeq; WP_066858465.1; NZ_LXVX01000008.1.
DR AlphaFoldDB; A0A196MNK6; -.
DR STRING; 453246.A7Q26_17210; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000078322; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000078322}.
FT DOMAIN 23..327
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 117..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 36056 MW; E2B01BC1E9CFB993 CRC64;
MARKPRPAKP RVIVTRRLPP NVEARMAELF DASFNVGDVA LSRTELARAM AQCDVLVPTI
SDQIDASLIE GAPDRLQLIA SFGSGVDHID LAAARRKGVI VTNTPGVLTE DTADMTMALI
LSVPRRLAEG EKLVRTGEWR GWSPSGMLGH RIGGKKLGII GMGRIGRAVA RRARAFGLSI
AYHNRHRLPF EVEQELEAVW HGELDMLLAS SDILSIHCPL NADSRGMIDA RRIALLGADA
YIINTSRAEV TDEDALIVAL EEGRIAGAGF DVYTHEPAVN PRLLALSNVT LLPHMGSATF
EGRDATGARV IANIRTWVDG HRPPNQVLEG WV
//
