ID A0A091C5Z5_9ENTE Unreviewed; 316 AA.
AC A0A091C5Z5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KFN91527.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:KFN91527.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:KFN91527.1};
GN ORFNames=TMU3MR103_0992 {ECO:0000313|EMBL:KFN91527.1};
OS Tetragenococcus muriaticus 3MR10-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Tetragenococcus.
OX NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN91527.1, ECO:0000313|Proteomes:UP000029381};
RN [1] {ECO:0000313|EMBL:KFN91527.1, ECO:0000313|Proteomes:UP000029381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN91527.1,
RC ECO:0000313|Proteomes:UP000029381};
RA Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT "Genome sequence of Tetragenococcus muriaticus.";
RL Submitted (AUG-2014) 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:KFN91527.1}.
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DR EMBL; JPVT01000090; KFN91527.1; -; Genomic_DNA.
DR RefSeq; WP_038022915.1; NZ_JPVT01000090.1.
DR AlphaFoldDB; A0A091C5Z5; -.
DR PATRIC; fig|1302648.3.peg.962; -.
DR Proteomes; UP000029381; Unassembled WGS sequence.
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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000029381}.
FT DOMAIN 27..314
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 316 AA; 35140 MW; 748C4EF796E64647 CRC64;
MNDKTVVLNG SVVNFDGNVD YSNIASEVVV YDQTPEDKIL ERVDEFNIVV TKEMPVPGDI
IRQFPDSVKM ICEAGTGFNN IDMDAVHEKG IALCNIPAYS TQRVAHTGIM FILNLASSMQ
KQIRMLEEGN HDNFQKHLMV NHMEVNGKTL GVIGYGNVGQ EIIKIAQALG MKILVSTRTP
RQDQDGVHFT TKEELFRQSD FVSLNCPLNE ETKHTVNEDT LAMMKPTAYL INTARGGLVD
ENALIQAIQN GVIAGAGLDV QEKEPLPDDS PLYDMEDVIV TPHMGWRGLE TRQRLVSLIQ
DNIQAFAKSE PINRVD
//
