ID LDHA_CORNI Reviewed; 332 AA. AC O93401; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 57. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27; GN Name=ldha; OS Coryphopterus nicholsi (Blackeye goby) (Rhinogobiops nicholsii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Gobioidei; OC Gobiidae; Gobiinae; Coryphopterus. OX NCBI_TaxID=79888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Muscle; RX PubMed=9319749; RA Fields P., Somero G.; RT "Amino acid sequence differences cannot fully explain interspecific RT variation in thermal sensitivities of gobiid fish A4-lactate RT dehydrogenases (A4-LDHs)."; RL J. Exp. Biol. 200:1839-1850(1997). 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; AF079534; AAC31199.1; -; mRNA. DR HSSP; P07195; 1I0Z. DR SMR; O93401; 2-332. DR HOVERGEN; O93401; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:EC. 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_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR001236; Lactate/malate_DH. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR016040; NAD(P)-bd_dom. 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 PRINTS; PR00086; LLDHDRGNASE. 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 2 332 L-lactate dehydrogenase A chain. FT /FTId=PRO_0000168433. FT NP_BIND 29 57 NAD (By similarity). FT ACT_SITE 193 193 Proton acceptor (By similarity). FT BINDING 99 99 NAD (By similarity). FT BINDING 106 106 Substrate (By similarity). FT BINDING 138 138 NAD or substrate (By similarity). FT BINDING 169 169 Substrate (By similarity). FT BINDING 248 248 Substrate (By similarity). SQ SEQUENCE 332 AA; 36221 MW; 745240067644A705 CRC64; MSTKEKLISH VSKEEAVGSR NKVTVVGVGM VGMASAISIL LKDLCDELAL VDVMEDKLKG EVMDLQHGSL FLKTHKIVGD KDYSVTANSR VVVVTAGARQ QEGESRLNLV QRNVNIFKFI IPNIVKYSPN CILMVVSNPV DILTYVAWKL SGFPRHRVIG SGTNLDSARF RHIMGEKLHL HPSSCHGWIV GEHGDSSVPV WSGVNVAGVS LQTLNPKMGA EGDSENWKAV HKMVVDGAYE VIKLKGYTSW AIGMSVADLV ESIVKNLHKV HPVSTLVKGM HGVKDEVFLS VPCVLGNSGL TDVIHMTLKA DEEKQLVKSA ETLWGVQKEL TL //