LDHA_CYPCA
ID LDHA_CYPCA Reviewed; 333 AA.
AC Q9W7K5;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=L-lactate dehydrogenase A chain;
DE Short=LDH-A;
DE EC=1.1.1.27;
GN Name=ldha;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
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 (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF076528; AAD40736.1; -; mRNA.
DR PDB; 1V6A; X-ray; 2.30 A; A/B=2-333.
DR PDBsum; 1V6A; -.
DR AlphaFoldDB; Q9W7K5; -.
DR SMR; Q9W7K5; -.
DR Ensembl; ENSCCRT00010024567; ENSCCRP00010022476; ENSCCRG00010009549.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; Q9W7K5; -.
DR Proteomes; UP000694384; Unplaced.
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; 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_0000168434"
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"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 107..128
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1V6A"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:1V6A"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:1V6A"
FT HELIX 311..328
FT /evidence="ECO:0007829|PDB:1V6A"
SQ SEQUENCE 333 AA; 36277 MW; 45B15E6943AD4024 CRC64;
MASTKEKLIT HVSKEEPAGP TNKVTVVGVG MVGMAAAISI LLKDLTDELA LVDVMEDKLK
GEAMDLQHGS LFLKTHKIVA DKDYSVTANS KVVVVTAGAR QQEGESRLNL VQRNVNIFKF
IIPNIIKYSP NCILLVVSNP VDILTYVAWK LSGLPRNRVI GSGTNLDSAR FRHLMGEKLG
IHPSNCHGWV IGEHGDSSVP VWSGVNVAGV FLQGLNPDMG TDKDKEDWKS VHKMVVDSAY
EVIKLKGYTS WAIGMSAADL CQSILKNLRK CHPVSTLVKG MHGVNEEVFL SVPCILGNSG
LTDVVHMTLK SDEEKQLVKS AETLWGVQKD LTL
