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Database: UniProt
Entry: A0A1H7LRR4_9FIRM
LinkDB: A0A1H7LRR4_9FIRM
Original site: A0A1H7LRR4_9FIRM 
ID   A0A1H7LRR4_9FIRM        Unreviewed;       310 AA.
AC   A0A1H7LRR4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:SEL01398.1};
GN   ORFNames=SAMN02910377_02427 {ECO:0000313|EMBL:SEL01398.1};
OS   Pseudobutyrivibrio ruminis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Pseudobutyrivibrio.
OX   NCBI_TaxID=46206 {ECO:0000313|EMBL:SEL01398.1, ECO:0000313|Proteomes:UP000182321};
RN   [1] {ECO:0000313|Proteomes:UP000182321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACV-9 {ECO:0000313|Proteomes:UP000182321};
RA   Varghese 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; FNZX01000018; SEL01398.1; -; Genomic_DNA.
DR   RefSeq; WP_074792111.1; NZ_FNZX01000018.1.
DR   AlphaFoldDB; A0A1H7LRR4; -.
DR   Proteomes; UP000182321; 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; PS00670; D_2_HYDROXYACID_DH_2; 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:UP000182321}.
FT   DOMAIN          14..309
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          106..287
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   310 AA;  34766 MW;  3A9121D5A82031B9 CRC64;
     MKIVFLDRKS IGEDIDLSCF NEFGEVVIYD YSTPEEAAER TVDADVVIIN KVPINENTIG
     KANNLKLVCV TATGTNNLDK DYLDKRNIAW RNVAGYSTEA VAQHTLALLL NLYEHLSYYD
     DYVKSEKYVN DKLFTHFEMH FNEIANKTWG IIGLGAIGKR VAEIATCLGA NVVYYSTSGK
     NHSDIYKEVD FDTLLSTSDV ISIHAPLDEN TLHLMDKNAF EKMKNSAILI NVGRGPIVVE
     KDLEDALESG QIAGAGLDVL DIEPMSPENP LRNIKDSNKL IITPHIAWAA VEARQRLMKI
     IYNQVKDYFN
//
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