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Database: UniProt
Entry: A0A0R1MCF5_9LACO
LinkDB: A0A0R1MCF5_9LACO
Original site: A0A0R1MCF5_9LACO 
ID   A0A0R1MCF5_9LACO        Unreviewed;       323 AA.
AC   A0A0R1MCF5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=FC81_GL001073 {ECO:0000313|EMBL:KRL01859.1};
OS   Liquorilactobacillus capillatus DSM 19910.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423731 {ECO:0000313|EMBL:KRL01859.1, ECO:0000313|Proteomes:UP000051621};
RN   [1] {ECO:0000313|EMBL:KRL01859.1, ECO:0000313|Proteomes:UP000051621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19910 {ECO:0000313|EMBL:KRL01859.1,
RC   ECO:0000313|Proteomes:UP000051621};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRL01859.1}.
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DR   EMBL; AZEF01000020; KRL01859.1; -; Genomic_DNA.
DR   RefSeq; WP_057743631.1; NZ_AZEF01000020.1.
DR   AlphaFoldDB; A0A0R1MCF5; -.
DR   STRING; 1423731.FC81_GL001073; -.
DR   PATRIC; fig|1423731.3.peg.1103; -.
DR   OrthoDB; 9802969at2; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000051621; 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; cd05291; HicDH_like; 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:UP000051621}.
FT   DOMAIN          9..146
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          149..316
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         14..19
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         39
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         44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         69
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         83..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         122..124
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         124..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         152..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         157
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         173
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         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   MOD_RES         224
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
SQ   SEQUENCE   323 AA;  34795 MW;  7516047FE0623783 CRC64;
     MSKTRNHQKV ILVGDGAVGS SYAYAMALQG VAEEFGIVDV VKERTEGDAL DLADATALSY
     PKRIYSAEYS DCKDANLVVI TAGAPQKPGE TRLDLVNKNL KILSSIVKPI VDSGFDGIFL
     VAANPVDILT YATWKFSGFP KDKVIGSGTS LDTSRLRVAL GELMGIQDPR SVHAYIMGEH
     GDSEFAAFSA ATVGGLPVLD WAKKNNVSKD QLDKLEDDVR NKAYEIISKK GATFYGVATA
     LARISKAILR DEDAVLPVSA YMEGQYGLND IYIGTPAVVN GNGLEKILEV PLNDEEAKKM
     TDSAATLKKV LNDGLKNLER MLN
//
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