ID LDHA_DISEL Reviewed; 331 AA. AC Q9PW61; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 25-NOV-2008, entry version 49. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27; GN Name=ldha; OS Dissostichus eleginoides (Patagonian toothfish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; OC Notothenioidei; Nototheniidae; Dissostichus. OX NCBI_TaxID=100907; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Muscle; RA Marshall C.J., McInnes S.J., Love C.A.; RT "Cold adaptation in lactate dehydrogenases from Antarctic fish."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)- CC lactate from pyruvate: step 1/1. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH 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; AF170027; AAD48482.1; -; mRNA. DR HSSP; P00339; 9LDT. DR SMR; Q9PW61; 2-331. DR HOVERGEN; Q9PW61; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro. DR GO; GO:0019642; P:anaerobic glycolysis; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001557; L-lactate/malate_DHase. DR InterPro; IPR011304; L-lactate_DHase. DR InterPro; IPR001236; Lactate/malate_DHase. DR InterPro; IPR015955; Lactate_DHase/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1. DR PROSITE; PS00064; L_LDH; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Glycolysis; NAD; Oxidoreductase. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 331 L-lactate dehydrogenase A chain. FT /FTId=PRO_0000168435. FT NP_BIND 29 57 NAD (By similarity). FT ACT_SITE 192 192 Proton acceptor (By similarity). FT BINDING 98 98 NAD (By similarity). FT BINDING 105 105 Substrate (By similarity). FT BINDING 137 137 NAD or substrate (By similarity). FT BINDING 168 168 Substrate (By similarity). FT BINDING 247 247 Substrate (By similarity). SQ SEQUENCE 331 AA; 36144 MW; 3AA5EDF03766FE65 CRC64; MSTKEKLISH VMKEEPVGSR NKVTVVGVGM VGMASAISIL LKDLCDELAM VDVMEDKLKG EVMDLQHGSL FLKTKIVGDK DYSVTANSKV VVVTAGARQQ EGESRLNLVQ RNVNIFKFII PNIVKYSPNC ILMVVSNPVD ILTYVAWKLS GFPRNRVIGS GTNLDSARFR HLIGEKLHLH PSSCHAWIVG EHGDSSVPVW SGVNVAGVSL QGLNPQMGTE GDGENWKAIH KEVVDGAYEV IKLKGYTSWA IGMSVADLVE SIIKNMHKVH PVSTLVQGMH GVKDEVFLSV PSVLGNSGLT DVIHMTLKAE EEKQLQKSAE TLWGVQKELT L //