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Database: UniProt
Entry: A0A142L252_9BACT
LinkDB: A0A142L252_9BACT
Original site: A0A142L252_9BACT 
ID   A0A142L252_9BACT        Unreviewed;       321 AA.
AC   A0A142L252;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AMS26298.1};
GN   ORFNames=AEM51_03930 {ECO:0000313|EMBL:AMS26298.1};
OS   Bacteroidetes bacterium UKL13-3.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1690483 {ECO:0000313|EMBL:AMS26298.1, ECO:0000313|Proteomes:UP000075224};
RN   [1] {ECO:0000313|Proteomes:UP000075224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Driscoll C.B.;
RL   Submitted (JUL-2015) 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; CP012155; AMS26298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142L252; -.
DR   STRING; 1690483.AEM51_03930; -.
DR   KEGG; bbau:AEM51_03930; -.
DR   PATRIC; fig|1690483.4.peg.836; -.
DR   Proteomes; UP000075224; Chromosome.
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; cd05303; PGDH_2; 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; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075224}.
FT   DOMAIN          8..320
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          130..297
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   321 AA;  34493 MW;  54AD4EAD5EA874DB CRC64;
     MTKILANDGI DANGKKILEA AGFTVDTTKI TQEKLATELN NYDAILVRSA TKVREDLIDA
     CPNLKLIGRG GVGMDNIDVA YAKNKGIAVI NTPASSSVSV AELVFAHIFS GSRFIQITNR
     VMPSKGNEEF GNLKKIASNG IELQGKTMGV YGFGRIGQEV AKIAIGLGMK VLAFDPYVET
     LDLIVNLPAL GENSRIKVNI KTVSEESVIT HSDFITFHVP FNEGDKAIID AAKMAKMKKG
     VGLINCSRGG VISETDLLAN LNSGHVAFAG LDVFEKEPPV NMDILQHDHV SVSPHIGGST
     IEAQNRIGIE LAEKVIEFFK K
//
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