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Database: UniProt
Entry: A0A1K1PD80_RUMFL
LinkDB: A0A1K1PD80_RUMFL
Original site: A0A1K1PD80_RUMFL 
ID   A0A1K1PD80_RUMFL        Unreviewed;       326 AA.
AC   A0A1K1PD80;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:SFW45411.1};
GN   ORFNames=SAMN02910280_2657 {ECO:0000313|EMBL:SFW45411.1};
OS   Ruminococcus flavefaciens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1265 {ECO:0000313|EMBL:SFW45411.1, ECO:0000313|Proteomes:UP000183461};
RN   [1] {ECO:0000313|EMBL:SFW45411.1, ECO:0000313|Proteomes:UP000183461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL228 {ECO:0000313|EMBL:SFW45411.1,
RC   ECO:0000313|Proteomes:UP000183461};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FPIP01000008; SFW45411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1PD80; -.
DR   Proteomes; UP000183461; 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; cd12183; LDH_like_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; IPR029753; D-isomer_DH_CS.
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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR   PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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}.
FT   DOMAIN          3..323
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          109..293
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   326 AA;  36109 MW;  2AD2A24342832AB0 CRC64;
     MKVAFFDTKQ YDMPSFEKLG KENNIKFKFY ETKLNEDTAA LAKGCEAVCV FVNDTVNAAV
     IDRLCELGVK VLALRCAGYN NVDIKYAKDK LKVVSVPAYS PYAVAEHAMA LLLTSIRRVH
     KAFIRTRDHN FSLNGLTGFD LHGKTVGVVG TGKIGRIFIN ICHGFGMNVI AYDKFPAKDS
     DIDYVELDEL FSRSDIISFH CPLTEETYHM IDSKSIDKLK KGVVIVNTSR GALIDAEALL
     EGIKARKIGA ACLDVYEEEA DVFFQDFSGH IIADDTLARL ISMPNVIVTS HQAFLTEEAL
     HNIAETTVSN ILACVKGEEC PNELHI
//
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