ID LDHA_CHICK Reviewed; 332 AA. AC P00340; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2008, entry version 67. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27; GN Name=LDHA; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91057138; PubMed=2243792; DOI=10.1093/nar/18.21.6432; RA Hirota Y., Katsumata A., Takeya T.; RT "Nucleotide and deduced amino acid sequences of chicken lactate RT dehydrogenase-A."; RL Nucleic Acids Res. 18:6432-6432(1990). RN [2] RP PROTEIN SEQUENCE OF 2-332. RA Torff H.-J., Becker D., Schwarzwalder J.; RL (In) Sund H. (eds.); RL Pyridine nucleotide dependent dehydrogenases, pp.31-42, Walter de RL Gruyter, Berlin (1977). 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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; X53828; CAA37824.1; -; mRNA. DR PIR; A00349; DECHLM. DR PIR; S12151; S12151. DR RefSeq; NP_990615.1; -. DR UniGene; Gga.4398; -. DR HSSP; P00338; 1I10. DR SMR; P00340; 2-332. DR Ensembl; ENSGALG00000006300; Gallus gallus. DR GeneID; 396221; -. DR KEGG; gga:396221; -. DR HOGENOM; P00340; -. DR HOVERGEN; P00340; -. 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 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 332 L-lactate dehydrogenase A chain. FT /FTId=PRO_0000168420. 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). FT CONFLICT 63 63 L -> M (in Ref. 2; AA sequence). FT CONFLICT 78 78 I -> T (in Ref. 2; AA sequence). FT CONFLICT 192 192 E -> Q (in Ref. 2; AA sequence). SQ SEQUENCE 332 AA; 36514 MW; 5ED8279CFAD7B62B CRC64; MSLKDHLIHN VHKEEHAHAH NKISVVGVGA VGMACAISIL MKDLADELTL VDVVEDKLKG EMLDLQHGSL FLKTPKIISG KDYSVTAHSK LVIVTAGARQ QEGESRLNLV QRNVNIFKFI IPNVVKYSPD CKLLIVSNPV DILTYVAWKI SGFPKHRVIG SGCNLDSARF RHLMGERLGI HPLSCHGWIV GEHGDSSVPV WSGVNVAGVS LKALHPDMGT DADKEHWKEV HKQVVDSAYE VIKLKGYTSW AIGLSVADLA ETIMKNLRRV HPISTAVKGM HGIKDDVFLS VPCVLGSSGI TDVVKMILKP DEEEKIKKSA DTLWGIQKEL QF //