LDH1_LACLC
ID LDH1_LACLC Reviewed; 325 AA.
AC P04034; P94885; P94886;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
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, ldhA;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ML1;
RX PubMed=8081494; DOI=10.1099/00221287-140-6-1301;
RA Swindell S.R., Griffin H.G., Gasson M.J.;
RT "Cloning, sequencing and comparison of three lactococcal L-lactate
RT dehydrogenase genes.";
RL Microbiology 140:1301-1305(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AM4, AM5, CM1-3, and MSUA2;
RX PubMed=9023947; DOI=10.1128/aem.63.2.694-702.1997;
RA Urbach E., Daniels B., Salama M.S., Sandine W.E., Giovannoni S.J.;
RT "The ldh phylogeny for environmental isolates of Lactococcus lactis is
RT consistent with rRNA genotypes but not with phenotypes.";
RL Appl. Environ. Microbiol. 63:694-702(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-22 AND 247-298.
RC STRAIN=US3;
RX PubMed=518918; DOI=10.1016/0005-2795(79)90254-x;
RA Crossley L.G., Jago G.R., Davidson B.E.;
RT "Partial sequence data for the L-(+)-lactate dehydrogenase from
RT Streptococcus cremoris US3 including the amino acid sequences around the
RT single cysteine residue and at the N-terminus.";
RL Biochim. Biophys. Acta 581:342-355(1979).
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; U02385; AAA61961.1; -; Genomic_DNA.
DR EMBL; U78630; AAB51674.1; -; Genomic_DNA.
DR EMBL; U78631; AAB51675.1; -; Genomic_DNA.
DR EMBL; U78633; AAB51677.1; -; Genomic_DNA.
DR EMBL; U78635; AAB51679.1; -; Genomic_DNA.
DR PIR; A20629; A20629.
DR RefSeq; WP_021165426.1; NZ_WJUX01000029.1.
DR AlphaFoldDB; P04034; -.
DR SMR; P04034; -.
DR SABIO-RK; P04034; -.
DR UniPathway; UPA00554; UER00611.
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 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 Allosteric enzyme; Cytoplasm; Direct protein sequencing; NAD;
KW Oxidoreductase; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:518918"
FT CHAIN 2..325
FT /note="L-lactate dehydrogenase 1"
FT /id="PRO_0000168354"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 43
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 82..83
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 121..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 123..126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 146
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 151..154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 156
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 171
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 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT MOD_RES 223
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT VARIANT 127
FT /note="I -> T (in strain: CM1-3)"
FT VARIANT 213
FT /note="K -> E (in strain: AM4 and CM1-3)"
FT VARIANT 293
FT /note="D -> E (in strain: AM4)"
FT CONFLICT 5
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="S -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 35050 MW; 6F50D8343AF13AA9 CRC64;
MADKQRKKVI LVGDGAVGSS YAFALVNQGI AQELGIVDLF KEKTQGDAED LSHALAFTSP
KKIYSADYSD ASDADLVVLT SGAPQKPGET RLDLVEKNLR ITKDVVTKIV ASGFKGIFLV
AANPVDILTY ATWKFSGFPK NRVVGSGTSL DTARFRQALA EKVDVDARSI HAYIMGEHGD
SEFAVWSHAN VAGVKLEQWF QENDYLNEAE IVKLFESVRD AAYSIIAKKG ATFYGVAVAL
ARITKAILDD EHAVLPVSVF QDGQYGVSDC YLGQPAVVGA EGVVNPIHIP LNDAEMQKME
ASGAQLKAII DEAFAKEEFA SAVKN
