LDHA_CHAGU
ID LDHA_CHAGU Reviewed; 331 AA.
AC O93541;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
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 Champsocephalus gunnari (Mackerel icefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Channichthyidae; Champsocephalus.
OX NCBI_TaxID=52237;
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; AF079824; AAC63282.1; -; mRNA.
DR PDB; 2V65; X-ray; 2.35 A; A/B=2-331.
DR PDBsum; 2V65; -.
DR AlphaFoldDB; O93541; -.
DR SMR; O93541; -.
DR BRENDA; 1.1.1.27; 9919.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; O93541; -.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000168431"
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"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 105..126
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 163..177
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:2V65"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 249..263
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:2V65"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2V65"
FT HELIX 309..327
FT /evidence="ECO:0007829|PDB:2V65"
SQ SEQUENCE 331 AA; 36156 MW; 556546DC3A03237E CRC64;
MSTKEKLISH VMKEEPVGSR SKVTVVGVGM VGMASAISIL 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 EEKQLQKSAE TLWGVQKELT L
