ID Q5YLI4_9LACO Unreviewed; 334 AA.
AC Q5YLI4;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:AAR19203.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:AAR19203.1};
GN Name=dldh {ECO:0000313|EMBL:AAR19203.1};
OS Lactobacillus sp. MONT4.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=244128 {ECO:0000313|EMBL:AAR19203.1};
RN [1] {ECO:0000313|EMBL:AAR19203.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MONT4 {ECO:0000313|EMBL:AAR19203.1};
RX PubMed=15466577; DOI=10.1128/AEM.70.10.6290-6295.2004;
RA Weekes J., Yuksel G.U.;
RT "Molecular characterization of two lactate dehydrogenase genes with a novel
RT structural organization on the genome of Lactobacillus sp. strain MONT4.";
RL Appl. Environ. Microbiol. 70:6290-6295(2004).
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; AY301012; AAR19203.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5YLI4; -.
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 9..332
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..301
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 334 AA; 37112 MW; BE03F2683A72889A CRC64;
MILKIVAYGI RADEKPYLNE WSKANPEVTV TSTGKLLDET TVDLAKEADG VVVYQQKPYT
ANVLNKLASY GVKNISLRNV GVDNIDATAV KQNGFKITNV PAYSPQAIAE FTVTELMRLL
RNTKTFDRKI ANGDLRWAPD VAEELNQMTV GVFATGRIGR AAIQIYRGFG AKIIAYDVFH
NPELEKEGIY VDTPEELYAK SDVLSIHAPA TKENEHMLND EAFSKMKDGV YILNPARGTL
VDTDALIRAL DAGKVKGAAL DVYEDEVGVF NTDFGSFDKI PDERLKNLLK RDNVLVTPHI
AFYTKKAVHN MVWFAMDANK SLIETGNSDK LVKF
//
