ID   LDHA_ELEMC              Reviewed;         332 AA.
AC   O93542;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, 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   Eleginops maclovinus (Patagonian blennie).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes;
OC   Notothenioidei; Eleginopidae; Eleginops.
OX   NCBI_TaxID=56733;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   MEDLINE=98409683; PubMed=9736762; DOI=10.1073/pnas.95.19.11476;
RA   Fields P.A., Somero G.N.;
RT   "Hot spots in cold adaptation: localized increases in conformational
RT   flexibility in lactate dehydrogenase A4 orthologs of Antarctic
RT   notothenioid fishes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:11476-11481(1998).
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.
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DR   EMBL; AF079825; AAC63283.1; -; mRNA.
DR   HSSP; P00336; 5LDH.
DR   SMR; O93542; 2-332.
DR   HOVERGEN; O93542; -.
DR   BRENDA; 1.1.1.27; 303898.
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_0000168437.
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;  36309 MW;  09A5245952011DAD CRC64;
     MSTKEKLISH VMKEEPVGSR NKVTVVGVGM VGMASAISIL LKDLCDELAM VDVMEDKLKG
     EVMDLQHGSL FLKTHKIVGD KDYSVTANSK LVVVTAGARQ QEGESRLNLV QRNVNIFKFI
     IPNIVKYSPN CILMVVSNPV DILTYVAWKL SGFPRHRVLG SGTNLDSARF RHLIGEKLNL
     HPSSCHAWII GEHGDSSVPV WSGLNVAGVS LQGLNPQMGT EGDSENWKAI HKEVVDGAYE
     VIKLKGYTSW AIGMSVADLV ESILKNLHKV HPVSTLVQGM HGVKDEVFLS VPCVLGNSGL
     TDVVHMTLKA EEEKQVQNSA ETLWGVQKEL TL
//