ID   LDHA_AMBME              Reviewed;         333 AA.
AC   Q9W7M6;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=L-lactate dehydrogenase A chain;
DE            Short=LDH-A;
DE            EC=1.1.1.27 {ECO:0000250|UniProtKB:P00338};
GN   Name=LDHA;
OS   Ambystoma mexicanum (Axolotl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Ambystomatidae; Ambystoma.
OX   NCBI_TaxID=8296;
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 gene
RT   duplication.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interconverts simultaneously and stereospecifically pyruvate
CC       and lactate with concomitant interconversion of NADH and NAD(+).
CC       {ECO:0000250|UniProtKB:P00338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC         Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC         Evidence={ECO:0000250|UniProtKB:P00338};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445;
CC         Evidence={ECO:0000250|UniProtKB:P00338};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23446;
CC         Evidence={ECO:0000250|UniProtKB:P00338};
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P00338}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000305}.
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DR   EMBL; AF070998; AAD40735.1; -; mRNA.
DR   AlphaFoldDB; Q9W7M6; -.
DR   SMR; Q9W7M6; -.
DR   UniPathway; UPA00554; UER00611.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_00488; Lactate_dehydrog; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR011304; L-lactate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..333
FT                   /note="L-lactate dehydrogenase A chain"
FT                   /id="PRO_0000168456"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         30..58
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  36631 MW;  EF97E41E545492C7 CRC64;
     MSCMKEQLII NILKDEHAPA QNKITVVGVG AVGMACAMSI LMKDLADELA LVDVIEDKLK
     GEMMDLQHGS LFLRTPKIVS GKDYSVTANS KLVIVTAGAR QQEGESRLNL VQRNVNIFKF
     IIPNVVKYSP DATLLVVSNP VDVLTYVAWK ISGFPKHRVI GSGCNLDSAR FRYLMGEKLG
     VHAQSCHGWV VGEHGDSSVP VWSGVNVAGV SLQTLNPELG TDADKENWKE VHKQVVESAY
     EVIKLKGYTS WAIGLSVADL AETIMKNLRR VHPVSTKVKG LYGVHEDVFL SVPCVLGNQG
     ITDVVKMTLK PEEEDRLRKS SDTLWGIQKE LHF