ID A0A139NSR4_9STRE Unreviewed; 333 AA.
AC A0A139NSR4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:KXT79060.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:KXT79060.1};
GN ORFNames=STRDD13_00249 {ECO:0000313|EMBL:KXT79060.1};
OS Streptococcus sp. DD13.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1777881 {ECO:0000313|EMBL:KXT79060.1, ECO:0000313|Proteomes:UP000070387};
RN [1] {ECO:0000313|EMBL:KXT79060.1, ECO:0000313|Proteomes:UP000070387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD13 {ECO:0000313|EMBL:KXT79060.1,
RC ECO:0000313|Proteomes:UP000070387};
RA Denapaite D., Rieger M., Koendgen S., Brueckner R., Ochigava I.,
RA Kappeler P., Maetz-Rensing K., Leendertz F., Hakenbeck R.;
RT "Highly variable Streptococcus oralis are common among viridans
RT streptococci isolated from primates.";
RL Submitted (JAN-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXT79060.1}.
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DR EMBL; LQRH01000010; KXT79060.1; -; Genomic_DNA.
DR RefSeq; WP_067100797.1; NZ_KQ969506.1.
DR AlphaFoldDB; A0A139NSR4; -.
DR STRING; 1777881.STRDD13_00249; -.
DR PATRIC; fig|1777881.3.peg.260; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000070387; Unassembled WGS sequence.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12184; HGDH_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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:KXT79060.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070387}.
FT DOMAIN 10..332
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..301
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 333 AA; 36684 MW; AC067C323D7DEEA5 CRC64;
MTLKVTCYGV RPNEVPFFEA LNKYGYELNL VEALTTHENA DAAKGSDAII LRGNCVADRE
NLEKWASWGI QYVFTRTVGF NHIDKEAAAA LGLKVAYVPG YSPNAIAELS LTLAMDLLRH
VSYTVNQTRQ LNFKVDATMF SKEIRNCKVG IIGTGRIGVT EAQLFKGLGA TVYGYDVFQS
EYAKSVVEFL ELDDLLATCD IVSLHVPYFK GQNDKMVNAE FISKMKDGAI LINTARGELQ
DNEAIVAAIK SGKLDGFGAD VLPNETAFFF KEFASKEDIP DATVREMIDL YPKILLTPHV
GSNTDEALSN MIETSYDNLN EVLTTGQLTN SVL
//
