ID LDHA_BOSMU Reviewed; 332 AA. AC A0A1F3; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 25-NOV-2008, entry version 13. DE RecName: Full=L-lactate dehydrogenase A chain; DE Short=LDH-A; DE EC=1.1.1.27; GN Name=LDHA; OS Bos mutus grunniens (Wild yak) (Bos grunniens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=30521; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Muscle; RA Zheng Y., He Q.; RT "Cloning and homology modeling of yak lactate dehydrogenase A."; RL Submitted (SEP-2006) 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; DQ991437; ABJ90429.1; -; mRNA. DR SMR; A0A1F3; 2-332. DR HOVERGEN; A0A1F3; -. 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 Acetylation; Cytoplasm; Glycolysis; NAD; Oxidoreductase; KW Phosphoprotein. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 332 L-lactate dehydrogenase A chain. FT /FTId=PRO_0000263071. FT NP_BIND 29 57 NAD (By similarity). FT ACT_SITE 193 193 Proton acceptor (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 MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 239 239 Phosphotyrosine (By similarity). SQ SEQUENCE 332 AA; 36686 MW; 0D854570222CC3F5 CRC64; MATLKDQLIQ NLLKEEHVPQ NKITIVGVGA VGMACAISIL MKDLADEVAL VDVMEDKLKG EMMDLQHGSL FLRTPKIVSG KDYNVTANSR LVIITAGARQ QEGESRLNLV QRNVNIFKFI IPNIVKYSPN CKLLVVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWIL GEHGDSSVPV WSGVNVAGVS LKNLHPELGT DADKEQWKAV HKQVVDSAYE VIKLKGYTSW AIGLSVVDLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI SDVVKVTLTH EEEAYLKKSA DTLWGIQKEL QF //