ID   LDHC_XENLA              Reviewed;         334 AA.
AC   P42121;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=L-lactate dehydrogenase C chain;
DE            Short=LDH-C;
DE            EC=1.1.1.27;
GN   Name=ldhc;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=7937776; DOI=10.1073/pnas.91.20.9392;
RA   Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L.;
RT   "Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals,
RT   birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from
RT   Xenopus, pig, and rat.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994).
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.
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; U07175; AAA50433.1; -; mRNA.
DR   PIR; I51654; I51654.
DR   RefSeq; NP_001165451.1; NM_001171980.1.
DR   AlphaFoldDB; P42121; -.
DR   SMR; P42121; -.
DR   BioGRID; 1078896; 1.
DR   GeneID; 100337512; -.
DR   CTD; 3948; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000186698; Genome assembly.
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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..334
FT                   /note="L-lactate dehydrogenase C chain"
FT                   /id="PRO_0000168487"
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         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   334 AA;  36277 MW;  8E24888668A0D0B2 CRC64;
     MSSVQENLIT NVCQDKAAKP TNKITIVGVG QVGMACAVSV LLKELADELA LVDILEDKLK
     GEVMDLQHGS LFLKTPTIVA DKDYSVTANS RIVVVTGGVR QQEGESALNL VQRNVNVFKF
     IIPQVVKYSP DCIIIVVSNP VDILTYVTWK LSGLPQHRII GSGTNLDSAR FRHLISEKLG
     VHPSSCHGFI LGEHGDTSVA VWSGVNVAGV SLQSLKPEIG TDQDSCNWKE VHKKVVDSAY
     EVIKLKGYTN WAIGFSVAEI VESITKNLGR VHPVSTMVKG MYGIETEVFL SLPCVLNGNG
     LTSVISQKLK DDEVGQLQKS SETLWGIQKD LQVL