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   03-AUG-2022, entry version 102.
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   Eleginops maclovinus (Patagonian blennie) (Eleginus maclovinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Eleginopidae; Eleginops.
OX   NCBI_TaxID=56733;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   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 notothenioid
RT   fishes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:11476-11481(1998).
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; AF079825; AAC63283.1; -; mRNA.
DR   AlphaFoldDB; O93542; -.
DR   SMR; O93542; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..332
FT                   /note="L-lactate dehydrogenase A chain"
FT                   /id="PRO_0000168437"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..57
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
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