ID   LDHA_XENLA              Reviewed;         334 AA.
AC   P42120; Q68EZ4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 122.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7937776; DOI=10.1073/pnas.91.20.9392;
RA   Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L.;
RT   "Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals,
RT   birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from
RT   Xenopus, pig, and rat.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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.
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; U07179; AAA50437.1; -; mRNA.
DR   EMBL; BC080054; AAH80054.1; -; mRNA.
DR   PIR; I51656; I51656.
DR   RefSeq; NP_001081050.1; NM_001087581.1.
DR   AlphaFoldDB; P42120; -.
DR   SMR; P42120; -.
DR   PRIDE; P42120; -.
DR   DNASU; 394355; -.
DR   GeneID; 394355; -.
DR   KEGG; xla:394355; -.
DR   CTD; 394355; -.
DR   Xenbase; XB-GENE-6254440; ldhb.L.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 394355; Expressed in heart and 20 other tissues.
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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..334
FT                   /note="L-lactate dehydrogenase A chain"
FT                   /id="PRO_0000168485"
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   334 AA;  36492 MW;  071EDA1E8A96540F CRC64;
     MASVQEKLIT CVCQDKPAKP TNKITIVGVG QVGMACAVSV LLKELADELA LVDILEDKLK
     GEMMDLQHGS LFLKTPTIVA DKDYSVTANS RIVVVTGGVR QQEGESRLNL VQRNVNIFKF
     IIPQIVKYSP DCIILVVSNP VDILTYVTWK LSGLPQHRII GSGTNLDSAR FRHLIAEKLG
     VHPTSCHGFI LGEHGDSSVA VWSGVNVAGV SLQSLKPDIG TDEDCCKWKE VHKQVVDSAY
     EVIKLKGYTN WAIGFSVAEI VESITKNLGR VHPVSTMVKG MYGIETEVFL SLPCVLNGNG
     LTSVINQKLK DNEVGQLQKS AETLWSIQKD LKDL