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Database: UniProt
Entry: A0A1H6X0U6_9FIRM
LinkDB: A0A1H6X0U6_9FIRM
Original site: A0A1H6X0U6_9FIRM 
ID   A0A1H6X0U6_9FIRM        Unreviewed;       330 AA.
AC   A0A1H6X0U6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:SEJ18195.1};
GN   ORFNames=SAMN05660742_10471 {ECO:0000313|EMBL:SEJ18195.1};
OS   Propionispira arboris.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Propionispira.
OX   NCBI_TaxID=84035 {ECO:0000313|EMBL:SEJ18195.1, ECO:0000313|Proteomes:UP000199662};
RN   [1] {ECO:0000313|EMBL:SEJ18195.1, ECO:0000313|Proteomes:UP000199662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2179 {ECO:0000313|EMBL:SEJ18195.1,
RC   ECO:0000313|Proteomes:UP000199662};
RA   de Groot N.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|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; FNZK01000004; SEJ18195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6X0U6; -.
DR   STRING; 84035.SAMN05660742_10471; -.
DR   Proteomes; UP000199662; 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; cd12185; HGDH_LDH_like; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199662}.
FT   DOMAIN          28..330
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..298
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   330 AA;  36693 MW;  9A1D744E415B8D2C CRC64;
     MQKPKICVFN YRDFDEGTYF EKISKELNIE LVICPTGPTK NSMGLAKDCQ CISIITTPID
     AELMEQLHLL GIKMISTRTI GFDHIDLAAA KKYDIAVSNA TYSTNGVADY AIMLMMMSAR
     KMKHIMQRAN IQDFSLRGLQ GREFAALTIG IIGTGKIGQT VIRHLSGFGN PILACSLYEC
     EDVKKYAQYV SLSELIQRSD IISLHTPLDE SNYHMINSKS IAAMKDQVIL VNTARGGLID
     TAALLDALES GKIGAAALDV IEDEFSLYYN DLKSQVLSNR NLAILRSYPN VIVTPHMAFY
     TDQDVHDMVY SSLKSCLLEI AGEKNPWRVN
//
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