ID LDHA_DANRE Reviewed; 333 AA. AC Q9PVK5; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 25-NOV-2008, entry version 59. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27; GN Name=ldha; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Tsoi S.C.-M., Li J.Y., Mannen H., Li S.S.-L.; RT "Molecular evolution of vertebrate lactate dehydrogenase isozymes by RT gene duplication."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (MAR-2004) 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; AF067201; AAF02212.1; -; mRNA. DR EMBL; BC067188; AAH67188.1; -; mRNA. DR RefSeq; NP_571321.1; -. DR UniGene; Dr.4212; -. DR HSSP; P00338; 1I10. DR SMR; Q9PVK5; 2-333. DR Ensembl; ENSDARG00000040856; Danio rerio. DR GeneID; 30496; -. DR KEGG; dre:30496; -. DR ZFIN; ZDB-GENE-991026-5; ldha. DR HOGENOM; Q9PVK5; -. DR HOVERGEN; Q9PVK5; -. 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 GO; GO:0001666; P:response to hypoxia; IDA:ZFIN. 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 Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 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 2 333 L-lactate dehydrogenase A chain. FT /FTId=PRO_0000168429. FT NP_BIND 30 58 NAD (By similarity). FT ACT_SITE 194 194 Proton acceptor (By similarity). FT BINDING 100 100 NAD (By similarity). FT BINDING 107 107 Substrate (By similarity). FT BINDING 139 139 NAD or substrate (By similarity). FT BINDING 170 170 Substrate (By similarity). FT BINDING 249 249 Substrate (By similarity). SQ SEQUENCE 333 AA; 36246 MW; B5A040A6DDC014BC CRC64; MASTKEKLIA HVSKEQPAGP TNKVTVVGVG MVGMAAAVSI LLKDLTDELA LVDVMEDKLK GEAMDLQHGS LFLKTHKIVA DKDYSVTANS KVVVVTAGAR QQEGESRLNL VQRNVNIFKF IIPNIIKYSP NCILLVVSNP VDILTYVAWK LSGLPRNRVI GSGTNLDSAR FRYLMGEKLG IHPSSCHGWV VGEHGDSSVP VWSGVNVAGV SLQALNPDLG TDKDKEDWKS VHKMVVDSAY EVIKLKGYTS WAIGMSVADL CESILKNMHK CHPVSTLVKG MHGVNEEVFL SVPCILGNNG LTDVVHMTLK PEEEKQLVKS AETLWGVQKE LTL //