ID LDHA_TREBE Reviewed; 331 AA. AC P69082; O93619; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 04-NOV-2026, entry version 84. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27 {ECO:0000250|UniProtKB:P00338}; GN Name=ldha; OS Trematomus bernacchii (Emerald rockcod) (Pseudotrematomus bernacchii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Trematomus. OX NCBI_TaxID=40690; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Muscle; RA Marshall C.J., Sharpe M.L., Love C.A.; RT "Cold adaptation in lactate dehydrogenases from Antarctic fish."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Interconverts simultaneously and stereospecifically pyruvate CC and lactate with concomitant interconversion of NADH and NAD(+). CC {ECO:0000250|UniProtKB:P00338}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-lactate + NAD(+) = pyruvate + NADH + H(+); CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; CC Evidence={ECO:0000250|UniProtKB:P00338}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445; CC Evidence={ECO:0000250|UniProtKB:P00338}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446; CC Evidence={ECO:0000250|UniProtKB:P00338}; CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate CC from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P00338}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF170847; AAD48487.1; -; mRNA. DR RefSeq; XP_033997584.1; XM_034141693.1. DR SMR; P69082; -. DR GeneID; 117491622; -. DR KEGG; tben:117491622; -. DR CTD; 3939; -. DR OrthoDB; 5405561at2759; -. DR UniPathway; UPA00554; UER00611. DR CDD; cd05293; LDH_1; 1. DR FunFam; 3.40.50.720:FF:000029; L-lactate dehydrogenase A chain; 1. DR FunFam; 3.90.110.10:FF:000003; L-lactate dehydrogenase A chain; 1. DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00488; Lactate_dehydrog; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR011304; L-lactate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1. DR PANTHER; PTHR43128:SF10; L-LACTATE DEHYDROGENASE A CHAIN; 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 SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR NCBIfam; TIGR01771; L-LDH-NAD; 1. DR NCBIfam; NF000824; PRK00066.1; 1. DR NCBIfam; NF004863; PRK06223.1; 1. DR PROSITE; PS00064; L_LDH; 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004459; F:L-lactate dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0006089; P:lactate metabolic process; IEA:TreeGrafter. DR AlphaFoldDB; P69082; -. PE 2: Evidence at transcript level; KW Cytoplasm; NAD; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..331 FT /note="L-lactate dehydrogenase A chain" FT /id="PRO_0000168446" FT ACT_SITE 192 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 31 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P00338" FT BINDING 52 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P00338" FT BINDING 98 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P00338" FT BINDING 105 FT /ligand="(S)-lactate" FT /ligand_id="ChEBI:CHEBI:16651" FT /evidence="ECO:0000250|UniProtKB:P00338" FT BINDING 135 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P00338" FT BINDING 137 FT /ligand="(S)-lactate" FT /ligand_id="ChEBI:CHEBI:16651" FT /evidence="ECO:0000250|UniProtKB:P00338" FT BINDING 137 FT /ligand="NADH" FT /ligand_id="ChEBI:CHEBI:57945" FT /evidence="ECO:0000250|UniProtKB:P00338" FT BINDING 168 FT /ligand="(S)-lactate" FT /ligand_id="ChEBI:CHEBI:16651" FT /evidence="ECO:0000250|UniProtKB:P00338" FT BINDING 247 FT /ligand="(S)-lactate" FT /ligand_id="ChEBI:CHEBI:16651" FT /evidence="ECO:0000250|UniProtKB:P00338" 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 //