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 25-NOV-2008, entry version 65. DE RecName: Full=D-lactate dehydrogenase; DE Short=D-LDH; DE EC=1.1.1.28; DE AltName: Full=D-specific D-2-hydroxyacid dehydrogenase; OS Lactobacillus helveticus. OC Bacteria; Firmicutes; 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 / IFO 15019 / JCM 1120 / Lh12; RX MEDLINE=93011111; PubMed=1396685; RA Kochhar S., Hottinger H., Chuard N., Taylor P.G., Atkinson T., RA Scawen M.D., 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 MEDLINE=94338682; PubMed=7765104; DOI=10.1007/s002530050169; 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., RA Holbrook J.J.; RL Submitted (OCT-1995) to the PDB data bank. CC -!- CATALYTIC ACTIVITY: (R)-lactate + NAD(+) = pyruvate + NADH. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X66723; CAA47255.1; -; Genomic_DNA. DR EMBL; U07604; AAA20464.1; -; Genomic_DNA. DR PIR; S29296; S29296. DR PDB; 2DLD; X-ray; 2.70 A; A/B=1-337. DR PDBsum; 2DLD; -. DR LinkHub; P30901; -. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006139; D-isomer_2_OHA_DHase. DR InterPro; IPR006140; D-isomer_2_OHA_DHase_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 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 1 Removed. FT CHAIN 2 337 D-lactate dehydrogenase. FT /FTId=PRO_0000075954. FT ACT_SITE 236 236 FT ACT_SITE 265 265 FT ACT_SITE 297 297 Proton donor. FT STRAND 3 8 FT TURN 11 13 FT HELIX 14 23 FT STRAND 28 30 FT HELIX 40 43 FT STRAND 48 52 FT HELIX 60 67 FT TURN 68 70 FT STRAND 73 75 FT STRAND 77 79 FT HELIX 86 91 FT HELIX 104 120 FT HELIX 122 130 FT HELIX 144 146 FT STRAND 147 152 FT HELIX 156 167 FT STRAND 171 175 FT HELIX 183 186 FT HELIX 193 196 FT TURN 197 199 FT STRAND 201 205 FT TURN 211 215 FT HELIX 219 222 FT STRAND 229 233 FT HELIX 237 239 FT HELIX 242 250 FT STRAND 253 260 FT HELIX 265 268 FT HELIX 281 288 FT STRAND 292 294 FT HELIX 303 322 FT STRAND 327 329 FT TURN 333 335 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 //