LDHC_FUNHE
ID LDHC_FUNHE Reviewed; 334 AA.
AC Q06176;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=L-lactate dehydrogenase C chain;
DE Short=LDH-C;
DE EC=1.1.1.27;
GN Name=ldhc;
OS Fundulus heteroclitus (Killifish) (Mummichog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus.
OX NCBI_TaxID=8078;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8419929; DOI=10.1073/pnas.90.1.242;
RA Quattro J.M., Woods H.A., Powers D.A.;
RT "Sequence analysis of teleost retina-specific lactate dehydrogenase C:
RT evolutionary implications for the vertebrate lactate dehydrogenase gene
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:242-246(1993).
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 -!- TISSUE SPECIFICITY: Eye and liver.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; L07336; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A47180; A47180.
DR AlphaFoldDB; Q06176; -.
DR SMR; Q06176; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000265000; Whole Genome Shotgun 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.
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_0000168484"
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"
SQ SEQUENCE 334 AA; 36575 MW; 6C353CAB1E7938D3 CRC64;
MASVLHKLIT PLACSSPEPP RNKVTVVGVG QVGMACAVTI LLRELADELA LVDVVEDKVK
GEMMDLQHGS LFLKTPKIVA DKDYSVTSNS RIVVVTAGVR QQEGERRLNL DQRNVNIFKH
IIPLIVRHSP DCIIIVVSNP VDVLTYVTWK LSGLPMHRVI GSGTNLDSAR FRFLMADKLG
IHSSSFNGWI LGEHGDTSVP VWSGTNVAGV NLQTLNPNIG TDFDEENWKE THKMVVDSAY
EVIKLKGYTN WAIGLSVADL TESLMRNMNR IHPVSTMAKG MYGIGDEVYL SLPCVLNSGG
VGSVVNMTLT DEEVAQLQGS ASTLWDIQKD LRDI
