ID LDHA_CHIRA Reviewed; 331 AA. AC P69081; O93619; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 25-NOV-2008, entry version 27. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27; GN Name=ldha; OS Chionodraco rastrospinosus (Ocellated icefish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; OC Notothenioidei; Channichthyidae; Chionodraco. OX NCBI_TaxID=34790; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Muscle; RX MEDLINE=98409683; PubMed=9736762; DOI=10.1073/pnas.95.19.11476; RA Fields P.A., Somero G.N.; RT "Hot spots in cold adaptation: localized increases in conformational RT flexibility in lactate dehydrogenase A4 orthologs of Antarctic RT notothenioid fishes."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11476-11481(1998). 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; AF079829; AAC63287.1; -; mRNA. DR HSSP; P00336; 5LDH. DR SMR; P69081; 2-331. DR HOVERGEN; P69081; -. 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_0000168432. 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; 36183 MW; 6C626409CA0FDAE9 CRC64; MSTKEKLISH VMKEEPVGSR NKVTVVGVGM VGMASAISIL LKDLCDELAM VDVMEDKLKG EVMDLQHGSL FLKTKIVGDK DYSVTANSKV VVVTAGARQQ EGESRLNLVQ RNVNIFKFII PNIVKYSPNC ILMVVSNPVD ILTYVAWKLS GFPRHRVIGS GTNLDSARFR HLIGEKLHLH PSSCHAWIVG EHGDSSVPVW SGVNVAGVSL QGLNPQMGTE GDGENWKAIH KEVVDGAYEV IKLKGYTSWA IGMSVADLVE SIIKNMHKVH PVSTLVQGMH GVKDEVFLSV PCVLGNSGLT DVIHMTLKAE EEKQLQKSAE TLWGVQKELT L //