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Database: UniProt
Entry: LDH1_CLOAB
LinkDB: LDH1_CLOAB
Original site: LDH1_CLOAB 
ID   LDH1_CLOAB              Reviewed;         313 AA.
AC   Q97MD1;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=L-lactate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00488};
DE            Short=L-LDH 1 {ECO:0000255|HAMAP-Rule:MF_00488};
DE            EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN   Name=ldh1 {ECO:0000255|HAMAP-Rule:MF_00488}; Synonyms=ldh;
GN   OrderedLocusNames=CA_C0267;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC       {ECO:0000255|HAMAP-Rule:MF_00488}.
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:0000255|HAMAP-Rule:MF_00488};
CC   -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC       bisphosphate (FBP). {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305}.
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DR   EMBL; AE001437; AAK78248.1; -; Genomic_DNA.
DR   PIR; E96932; E96932.
DR   RefSeq; NP_346908.1; NC_003030.1.
DR   RefSeq; WP_010963590.1; NC_003030.1.
DR   AlphaFoldDB; Q97MD1; -.
DR   SMR; Q97MD1; -.
DR   STRING; 272562.CA_C0267; -.
DR   GeneID; 44996763; -.
DR   KEGG; cac:CA_C0267; -.
DR   PATRIC; fig|272562.8.peg.453; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_1_1_9; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 9802969at2; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05292; LDH_2; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
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; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..313
FT                   /note="L-lactate dehydrogenase 1"
FT                   /id="PRO_0000168333"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         41
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         66
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         80..81
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         102
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         119..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         121..124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         144
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         149..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         154
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         169
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   MOD_RES         222
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
SQ   SEQUENCE   313 AA;  34181 MW;  C98FD402E62F45D2 CRC64;
     MKKNTKISVI GAGFVGSSTV FALMNGGLAS EIVIVDVNKD KAEGEAMDLS HGAAFVKPVV
     VKSGDYKDTE GSDIVIITAG AAQKPGETRL ELINKNYNIF KSIVPEVVKY NPNAILLVVS
     NPVDILTYIT YKLSGFPKSR VIGSGTVLDT SRFRYMLSEH FEIDVRNIHT YIMGEHGDSE
     IATWSLTNIA GMDVNEYCEA SCKKCDGSLK YKIYDDVKNA AYHVIEKKGA TYYAVALAVK
     RIVEAILRDE NSILTVSSLL EGQYGIKDVY MGVPSIVGIN GVKDIIEVPL NDEEKNNLTD
     SAKTLKESLD SIF
//
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