ID A0A068QP20_9GAMM Unreviewed; 312 AA.
AC A0A068QP20;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:CDG16708.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:CDG16708.1};
GN ORFNames=XDD1_1005 {ECO:0000313|EMBL:CDG16708.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG16708.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG16708.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; FO704550; CDG16708.1; -; Genomic_DNA.
DR RefSeq; WP_045969125.1; NZ_VNHN01000134.1.
DR AlphaFoldDB; A0A068QP20; -.
DR STRING; 351671.XDD1_1005; -.
DR KEGG; xdo:XDD1_1005; -.
DR HOGENOM; CLU_019796_1_3_6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000032721; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 7..300
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 35409 MW; 716316691D43FFBD CRC64;
MASKLKILIV DPIHIKLKNY MERNFTITVK HPITQQELIN CIKKYDILVL RSGAQINNQF
LEQAKHLRAI IRAGTGIDNI DLQALSKTDI LFYNTPSTNS RAVAELSFSL MHCLFRHIKR
ASTEIESNIW NKKLLMGFEL KNKNLGLIGF GSIGQEIARI AKGYDMQVSC TVSHYTAERA
ADMKKKDITL FDDLNVLMAF NDILVVCCPY TESTKNLLNK NNLCHLQPTS ILINVARGGV
VSEQDLYQSL ANRDIYGAAS DVFEYERQFS PLFTLDNFIG TPHIGAMTNE SQEKIADLII
RFLEEKLLKE VY
//
