ID   Q4L921_STAHJ            Unreviewed;       330 AA.
AC   Q4L921;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=D-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00014095};
DE            EC=1.1.1.28 {ECO:0000256|ARBA:ARBA00012969};
DE   AltName: Full=D-specific 2-hydroxyacid dehydrogenase {ECO:0000256|ARBA:ARBA00030947};
GN   Name=ddh {ECO:0000313|EMBL:BAE03854.1};
GN   OrderedLocusNames=SH0545 {ECO:0000313|EMBL:BAE03854.1};
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE03854.1, ECO:0000313|Proteomes:UP000000543};
RN   [1] {ECO:0000313|EMBL:BAE03854.1, ECO:0000313|Proteomes:UP000000543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE03854.1,
RC   ECO:0000313|Proteomes:UP000000543};
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC         Xref=Rhea:RHEA:16369, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16004, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001303};
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; AP006716; BAE03854.1; -; Genomic_DNA.
DR   RefSeq; WP_011274870.1; NC_007168.1.
DR   AlphaFoldDB; Q4L921; -.
DR   KEGG; sha:SH0545; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_1_9; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd12186; LDH; 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          23..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;  36415 MW;  68416525C8A1AF7E CRC64;
     MTKIMFYGTR DYEKNDALNW GKANNVEVVT TEEILSEDTV DLAKGFDGVT TMQFGKLADS
     VYPKLEEYGI KQIAQRTAGF DMYDLELAKK HGIIISNVPS YSPETIAEYS VSIALQLVRR
     FPAIEKRVQE HNFKWAAPIM STPVKNMTVA IIGTGRIGAA TGKIYAGFGA KVVGYDAYPN
     NSLDFLEYKD TVEEAIADAD IISLHVPANK ESFHLFDADM FSKVKKGAVL VNAARGAVID
     TPELIKAIND GTLYGAAIDT YENEAPYFTY DWTGKEIEDE TLLELIKHEN ILVTPHIAFF
     SDEAVRNLVE GGLNAALSVI NTGKCETQLN
//