ID   LDHA_NOTNE              Reviewed;         331 AA.
AC   O93539;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 105.
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   Notothenia neglecta (Yellowbelly rockcod) (Notothenia coriiceps neglecta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Notothenia.
OX   NCBI_TaxID=202063;
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; AF079822; AAC63280.1; -; mRNA.
DR   AlphaFoldDB; O93539; -.
DR   SMR; O93539; -.
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..331
FT                   /note="L-lactate dehydrogenase A chain"
FT                   /id="PRO_0000168445"
FT   ACT_SITE        192
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         98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  36167 MW;  0E25E52A053D0E5A CRC64;
     MSTKEKLISH VMKEEPVGSR NKVTVVGVGM VGMASAVSIL LKDLCDELAM VDVMEDKLKG
     EVMDLQHGSL FLKTKIVGDK DYSVTANSKV VVVTAGARQQ EGESRLNLVQ RNVNIFKFII
     PNIVKYSPNC ILMVVSNPVD ILTYVAWKLS GFPRHRVIGS GTNLDSARFR HLIGEKLHLH
     PSSCHAWIVG EHGDSSVPVW SGVNVAGVSL QGLNPQMGTE GDGENWKAIH KEVVDGAYEV
     IKLKGYTSWA IGMSVADLVE SIIKNMHKVH PVSTLVQGMH GVKDEVFLSV PCVLGNSGLT
     DVIHMTLKAE EEKQVQKSAE TLWGVQKELI L