ID   LDHA_DANRE              Reviewed;         333 AA.
AC   Q9PVK5;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 144.
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   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
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 (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-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. {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; AF067201; AAF02212.1; -; mRNA.
DR   EMBL; BC067188; AAH67188.1; -; mRNA.
DR   RefSeq; NP_571321.1; NM_131246.1.
DR   AlphaFoldDB; Q9PVK5; -.
DR   SMR; Q9PVK5; -.
DR   STRING; 7955.ENSDARP00000059885; -.
DR   PaxDb; Q9PVK5; -.
DR   Ensembl; ENSDART00000163892; ENSDARP00000137433; ENSDARG00000101251.
DR   Ensembl; ENSDART00000167542; ENSDARP00000140963; ENSDARG00000101251.
DR   GeneID; 30496; -.
DR   KEGG; dre:30496; -.
DR   CTD; 3939; -.
DR   ZFIN; ZDB-GENE-991026-5; ldha.
DR   eggNOG; KOG1495; Eukaryota.
DR   GeneTree; ENSGT00940000153201; -.
DR   HOGENOM; CLU_045401_0_2_1; -.
DR   InParanoid; Q9PVK5; -.
DR   OMA; SICKYIL; -.
DR   OrthoDB; 1204514at2759; -.
DR   PhylomeDB; Q9PVK5; -.
DR   TreeFam; TF314963; -.
DR   Reactome; R-DRE-70268; Pyruvate metabolism.
DR   UniPathway; UPA00554; UER00611.
DR   PRO; PR:Q9PVK5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 25.
DR   Bgee; ENSDARG00000101251; Expressed in swim bladder and 48 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0001666; P:response to hypoxia; IDA:ZFIN.
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..333
FT                   /note="L-lactate dehydrogenase A chain"
FT                   /id="PRO_0000168429"
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;  36246 MW;  B5A040A6DDC014BC CRC64;
     MASTKEKLIA HVSKEQPAGP TNKVTVVGVG MVGMAAAVSI LLKDLTDELA LVDVMEDKLK
     GEAMDLQHGS LFLKTHKIVA DKDYSVTANS KVVVVTAGAR QQEGESRLNL VQRNVNIFKF
     IIPNIIKYSP NCILLVVSNP VDILTYVAWK LSGLPRNRVI GSGTNLDSAR FRYLMGEKLG
     IHPSSCHGWV VGEHGDSSVP VWSGVNVAGV SLQALNPDLG TDKDKEDWKS VHKMVVDSAY
     EVIKLKGYTS WAIGMSVADL CESILKNMHK CHPVSTLVKG MHGVNEEVFL SVPCILGNNG
     LTDVVHMTLK PEEEKQLVKS AETLWGVQKE LTL