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Database: UniProt
Entry: D2Q5D7_BIFDB
LinkDB: D2Q5D7_BIFDB
Original site: D2Q5D7_BIFDB 
ID   D2Q5D7_BIFDB            Unreviewed;       320 AA.
AC   D2Q5D7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 88.
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=ldh2 {ECO:0000313|EMBL:ADB10152.1};
GN   Synonyms=ldh {ECO:0000256|HAMAP-Rule:MF_00488};
GN   OrderedLocusNames=BDP_1558 {ECO:0000313|EMBL:ADB10152.1};
OS   Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB10152.1, ECO:0000313|Proteomes:UP000008693};
RN   [1] {ECO:0000313|EMBL:ADB10152.1, ECO:0000313|Proteomes:UP000008693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC   {ECO:0000313|Proteomes:UP000008693};
RX   PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA   Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA   Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA   Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA   Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT   "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT   adaptation to the human oral cavity.";
RL   PLoS Genet. 5:E1000785-E1000785(2009).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00488}.
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DR   EMBL; CP001750; ADB10152.1; -; Genomic_DNA.
DR   RefSeq; WP_003839412.1; NC_013714.1.
DR   AlphaFoldDB; D2Q5D7; -.
DR   SMR; D2Q5D7; -.
DR   STRING; 401473.BDP_1558; -.
DR   GeneID; 69536311; -.
DR   KEGG; bde:BDP_1558; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_1_1_11; -.
DR   OMA; ASCAEYI; -.
DR   UniPathway; UPA00554; UER00611.
DR   Proteomes; UP000008693; 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 {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:UP000008693}.
FT   DOMAIN          9..148
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          151..314
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         15..20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         19
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         40
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         45
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         124..126
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         126..129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         154..157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   BINDING         159
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         174
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         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
FT   MOD_RES         228
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00488"
SQ   SEQUENCE   320 AA;  33980 MW;  E7E54612856ADC0E CRC64;
     MVDSPIKPTK LAIIGAGAVG STLAFAAAQR GVAREIVLED IAKERVEAEV LDMQHGSSFY
     PTVSIAGGDD PEICRDADMI VITAGPRQKP GQSRLELVGA TINILKAIIP GLVKVAPNAI
     FMLITNPVDI ATHVAQKISG LPKNQVFGSG TNLDSARLRF LIAQQTGVNV KNVHAYIAGE
     HGDSEVPLWA SATIGGVPMC DWTPLPGHDP LDADKREEIH QEVKNAAYKI INGKGATNYA
     IGMSGVDIIE AVMRDSNRIL PVSSMLEDFH GISDVCMSVP TLLNRSGVNT AINTPVSDRE
     LAALKRSAET LKETAAQFGF
//
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