ID   LDHA_FUNHE              Reviewed;         332 AA.
AC   Q92055;
DT   15-JUL-1999, 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;
DE   AltName: Full=LDH-M;
GN   Name=ldha;
OS   Fundulus heteroclitus (Killifish) (Mummichog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Atherinomorpha;
OC   Cyprinodontiformes; Fundulidae; Fundulus.
OX   NCBI_TaxID=8078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   MEDLINE=95400447; PubMed=7670598;
RA   Quattro J.M., Pollock D.D., Powell M., Woods H.A., Powers D.A.;
RT   "Evolutionary relations among vertebrate muscle-type lactate
RT   dehydrogenases.";
RL   Mol. Mar. Biol. Biotechnol. 4:224-231(1995).
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; L43525; AAA99462.1; -; mRNA.
DR   HSSP; P00336; 5LDH.
DR   SMR; Q92055; 2-332.
DR   HOVERGEN; Q92055; -.
DR   BRENDA; 1.1.1.27; 39477.
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_0000168438.
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;  36334 MW;  E518179F537C8D88 CRC64;
     MSTQEKLISH VMKEEPVGCR NKVTVVGVGM VGMASAISVL LKDLCDELAL VDVMEDKLKG
     EAMDLQHGAL FLKTHKIVAD KDYSVTANSK VVVVTAGARQ QEGESRLNLV QRNVNIFKFI
     IPNIVKYSPN CILLVVSNPV DILTYVAWKL SGFPRHRVIG SGTNLDSARF RHLMGEKFHL
     HPSSCHGWIV GEHGDSSVAV WSGVNIAGVS LQTLNPNMGA DGDSENWKEL HKKVVDGAYE
     VIKLKGYTSW AIGMSVADLV ESIVKNLHKV HPVSTLVQGM HGVKDEVFLS IPCVLGNSGL
     TDVIHMTLKP EEEKQLVKSA ETLWGVQKEL TL
//