LDHD_LACHE
ID LDHD_LACHE Reviewed; 337 AA.
AC P30901;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=D-lactate dehydrogenase;
DE Short=D-LDH;
DE EC=1.1.1.28;
DE AltName: Full=D-specific 2-hydroxyacid dehydrogenase;
OS Lactobacillus helveticus (Lactobacillus suntoryeus).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-36.
RC STRAIN=ATCC 15009 / DSM 20075 / BCRC 12936 / JCM 1120 / NBRC 15019 / NCIMB
RC 11971 / NRRL B-4526 / Lh12;
RX PubMed=1396685; DOI=10.1111/j.1432-1033.1992.tb17250.x;
RA Kochhar S., Hottinger H., Chuard N., Taylor P.G., Atkinson T., Scawen M.D.,
RA Nicholls D.J.;
RT "Cloning and overexpression of Lactobacillus helveticus D-lactate
RT dehydrogenase gene in Escherichia coli.";
RL Eur. J. Biochem. 208:799-805(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CNRZ 32;
RX PubMed=7765104; DOI=10.1007/bf00939032;
RA Bhowmik T.K., Steele J.L.;
RT "Cloning, characterization and insertional inactivation of the
RT Lactobacillus helveticus D(-) lactate dehydrogenase gene.";
RL Appl. Microbiol. Biotechnol. 41:432-439(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RA Bernard N., Delcour J., Alvarez A., Cortes A., Willis C., Holbrook J.J.;
RL Submitted (OCT-1995) to the PDB data bank.
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 -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; X66723; CAA47255.1; -; Genomic_DNA.
DR EMBL; U07604; AAA20464.1; -; Genomic_DNA.
DR PIR; S29296; S29296.
DR RefSeq; WP_003628108.1; NZ_WCGD01000045.1.
DR PDB; 2DLD; X-ray; 2.70 A; A/B=1-337.
DR PDBsum; 2DLD; -.
DR AlphaFoldDB; P30901; -.
DR SMR; P30901; -.
DR STRING; 326425.lhe_0073; -.
DR DrugBank; DB03940; Oxamic Acid.
DR GeneID; 66451111; -.
DR eggNOG; COG1052; Bacteria.
DR BRENDA; 1.1.1.28; 2870.
DR SABIO-RK; P30901; -.
DR EvolutionaryTrace; P30901; -.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1396685"
FT CHAIN 2..337
FT /note="D-lactate dehydrogenase"
FT /id="PRO_0000075954"
FT ACT_SITE 236
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 265
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 297
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 156..157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 207..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 234..236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2DLD"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:2DLD"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:2DLD"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:2DLD"
FT TURN 211..215
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:2DLD"
FT HELIX 303..322
FT /evidence="ECO:0007829|PDB:2DLD"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2DLD"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:2DLD"
SQ SEQUENCE 337 AA; 37779 MW; D0561DD82C03B3C4 CRC64;
MTKVFAYAIR KDEEPFLNEW KEAHKDIDVD YTDKLLTPET AKLAKGADGV VVYQQLDYTA
DTLQALADAG VTKMSLRNVG VDNIDMDKAK ELGFQITNVP VYSPNAIAEH AAIQAARVLR
QDKRMDEKMA KRDLRWAPTI GREVRDQVVG VVGTGHIGQV FMRIMEGFGA KVIAYDIFKN
PELEKKGYYV DSLDDLYKQA DVISLHVPDV PANVHMINDK SIAEMKDGVV IVNCSRGRLV
DTDAVIRGLD SGKIFGFVMD TYEDEVGVFN KDWEGKEFPD KRLADLIDRP NVLVTPHTAF
YTTHAVRNMV VKAFNNNLKL INGEKPDSPV ALNKNKF
