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Database: UniProt
Entry: R5CQ58_9FIRM
LinkDB: R5CQ58_9FIRM
Original site: R5CQ58_9FIRM 
ID   R5CQ58_9FIRM            Unreviewed;       323 AA.
AC   R5CQ58;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|HAMAP-Rule:MF_00488};
DE            Short=L-LDH {ECO:0000256|HAMAP-Rule:MF_00488};
DE            EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|HAMAP-Rule:MF_00488};
GN   Name=ldh {ECO:0000256|HAMAP-Rule:MF_00488};
GN   ORFNames=BN785_00570 {ECO:0000313|EMBL:CCX66862.1};
OS   Firmicutes bacterium CAG:791.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262993 {ECO:0000313|EMBL:CCX66862.1, ECO:0000313|Proteomes:UP000018038};
RN   [1] {ECO:0000313|EMBL:CCX66862.1, ECO:0000313|Proteomes:UP000018038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:791 {ECO:0000313|Proteomes:UP000018038};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC       {ECO:0000256|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:0000256|ARBA:ARBA00001763, ECO:0000256|HAMAP-
CC         Rule:MF_00488};
CC   -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC       bisphosphate (FBP). {ECO:0000256|HAMAP-Rule:MF_00488}.
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC       from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC       ECO:0000256|HAMAP-Rule:MF_00488}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00488}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054, ECO:0000256|HAMAP-Rule:MF_00488}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCX66862.1}.
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DR   EMBL; CAWT010000232; CCX66862.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5CQ58; -.
DR   STRING; 1262993.BN785_00570; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000018038; Unassembled WGS sequence.
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 {ECO:0000256|HAMAP-Rule:MF_00488};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00488};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00488};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00488}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00488};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018038}.
FT   DOMAIN          15..152
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          155..317
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         20..25
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         24
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         45
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         50
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         75
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         89..90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         128..130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         130..133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         153
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         158..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         163
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         178
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   MOD_RES         231
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
SQ   SEQUENCE   323 AA;  34937 MW;  AF87CF08BAD17F95 CRC64;
     MTAQREETNR TDNRKIAIIG CGFVGSASAF ALMQSGLFSE IALLDADKNR AEGEALDISH
     GVPFAGNVRV YAADYDDIID AGIIVVTAGA AQKPGETRLD LVHKNVSIFQ SIIPELKKRN
     YPGILLIVSN PVDILTLAAL RLSGFAENRV FGSGTVLDTA RLKTELGRHL SVDSRSVHSF
     IIGEHGDSEI VAWSSANVSG VPLSNFCEMR GHHQHEEAMR QIAENVKNSA YEIIEKKHAT
     YYGIAMSVVR ICRAVVMNER SILPVSSMMH GEYGVEGLAL SMPAIVGAEG VETHVPIVLS
     EGEQESLRRS AEALSRVVRE SGL
//
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