ID A0A1G9GD03_9GAMM Unreviewed; 313 AA.
AC A0A1G9GD03;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:SDK98520.1};
GN ORFNames=SAMN05661010_00668 {ECO:0000313|EMBL:SDK98520.1};
OS Halomonas muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=119000 {ECO:0000313|EMBL:SDK98520.1, ECO:0000313|Proteomes:UP000198654};
RN [1] {ECO:0000313|EMBL:SDK98520.1, ECO:0000313|Proteomes:UP000198654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14789 {ECO:0000313|EMBL:SDK98520.1,
RC ECO:0000313|Proteomes:UP000198654};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FNGI01000001; SDK98520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9GD03; -.
DR STRING; 119000.SAMN05661010_00668; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000198654; 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; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198654}.
FT DOMAIN 20..309
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 313 AA; 33534 MW; A3F417B71B2C825D CRC64;
MKAVILDAAS LGDDIDLSPL CNEVATLDVH AHSKPQECQA RLQDADIAIV NKVQLDGELL
SALPRLKLIC VLATGTNNID KAAAERHGIY VKNVNAYGTA SVAQHTMMLM LALANRLPLY
QRDVAAGRWD ESPIFCLLDH RTLELAGKRL VIVGSGELGQ AVARLAEAFS MDVVFAARPG
NEANDARPSL VELSPSADIL SLHCPLTEAT RHLIDADLLS RMKSDALVIN CARGGIVDER
AVLAALRRGQ LGGLGIDVLS QEPPREGLPL LDALSEPLNL IVTPHNAWIS PEARANVVRL
TAENLRAWAG TQG
//
