ID A0A120GD37_9SPHN Unreviewed; 338 AA.
AC A0A120GD37;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:KWV96103.1};
GN ORFNames=ASS64_02490 {ECO:0000313|EMBL:KWV96103.1};
OS Erythrobacter sp. AP23.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=499656 {ECO:0000313|EMBL:KWV96103.1, ECO:0000313|Proteomes:UP000058666};
RN [1] {ECO:0000313|EMBL:KWV96103.1, ECO:0000313|Proteomes:UP000058666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP23 {ECO:0000313|EMBL:KWV96103.1,
RC ECO:0000313|Proteomes:UP000058666};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. AP23.";
RL Submitted (NOV-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:KWV96103.1}.
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DR EMBL; LNBY01000001; KWV96103.1; -; Genomic_DNA.
DR RefSeq; WP_067689334.1; NZ_LNBY01000001.1.
DR AlphaFoldDB; A0A120GD37; -.
DR STRING; 499656.ASS64_02490; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000058666; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 19..333
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 125..302
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 338 AA; 36812 MW; 763E50C7E7DEAAC6 CRC64;
MESSETRPAK RLERTPRVVV TRHLMPFVEE RMGELFDVRL NTDDVPLTRE QLVAAMQDCD
VLVPTVTDRI DAEMLAQASA DLGLIANFGA GTEHLDLEAA ASRGIMVTNT PGVFTDDTAD
LAMAGIIGVP RRIREGVELI RSGKWSGWTP TALLGTKLAG KVLGIVGMGR IGQAVAHRAR
AFGLEIAYHN RKRLPEAVER MFQARWVESL DELMGEADIL TLHCPAGPGT HHMIDERRIG
LMKDGASLIN TARGDLVDQE ALIAALEGGR LAGAGLDVYP DEPNVDRRLI RHPNVMTLPH
IGSATREGRE ESGLKVIANI RMWADGHRPP DQVLTGLG
//
