LDH2_BIFL2
ID LDH2_BIFL2 Reviewed; 320 AA.
AC E8ME30; P19869; Q9L505; Q9L506;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=L-lactate dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:8450537};
DE Short=L-LDH 2 {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:8450537};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
DE AltName: Full=FBP-dependent LDH {ECO:0000303|PubMed:8450537};
GN Name=ldh2 {ECO:0000255|HAMAP-Rule:MF_00488}; OrderedLocusNames=BLLJ_1290;
OS Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM
OS 1217 / NCTC 11818 / E194b).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=565042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-233.
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RA Roy D., Sirois S.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=AM 101-2;
RX PubMed=8450537; DOI=10.1006/jmbi.1993.1122;
RA Iwata S., Ohta T.;
RT "Molecular basis of allosteric activation of bacterial L-lactate
RT dehydrogenase.";
RL J. Mol. Biol. 230:21-27(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD; SUBSTRATE ANALOG
RP AND FRUCTOSE 1,6-BISPHOSPHATE, ACTIVITY REGULATION, ACTIVE SITE, AND
RP SUBUNIT.
RC STRAIN=AM 101-2;
RX PubMed=7656036; DOI=10.1038/nsb0394-176;
RA Iwata S., Kamata K., Yoshida S., Ohta T.;
RT "T and R states in the crystals of bacterial L-lactate dehydrogenase reveal
RT the mechanism for allosteric control.";
RL Nat. Struct. Biol. 1:176-185(1994).
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 ECO:0000269|PubMed:7656036, ECO:0000305|PubMed:8450537}.
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 ECO:0000269|PubMed:7656036, ECO:0000269|PubMed:8450537}.
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; AP010888; BAJ66957.1; -; Genomic_DNA.
DR EMBL; AF261669; AAF70510.1; -; Genomic_DNA.
DR RefSeq; WP_007052533.1; NC_015067.1.
DR PDB; 1LLD; X-ray; 2.00 A; A/B=2-320.
DR PDB; 1LTH; X-ray; 2.50 A; R/T=2-320.
DR PDBsum; 1LLD; -.
DR PDBsum; 1LTH; -.
DR AlphaFoldDB; E8ME30; -.
DR SMR; E8ME30; -.
DR GeneID; 66505530; -.
DR KEGG; blm:BLLJ_1290; -.
DR HOGENOM; CLU_045401_1_1_11; -.
DR OMA; ASCAEYI; -.
DR BioCyc; MetaCyc:MON-13065; -.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; E8ME30; -.
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 3D-structure; Allosteric enzyme; Cytoplasm; NAD; Oxidoreductase;
KW Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..320
FT /note="L-lactate dehydrogenase 2"
FT /id="PRO_0000409353"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000305|PubMed:7656036, ECO:0007744|PDB:1LTH"
FT BINDING 18..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|PubMed:7656036, ECO:0000269|PubMed:8450537,
FT ECO:0007744|PDB:1LLD, ECO:0007744|PDB:1LTH"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|PubMed:7656036, ECO:0000269|PubMed:8450537,
FT ECO:0007744|PDB:1LLD, ECO:0007744|PDB:1LTH"
FT BINDING 45
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:7656036,
FT ECO:0000269|PubMed:8450537, ECO:0007744|PDB:1LLD,
FT ECO:0007744|PDB:1LTH"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 124..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|PubMed:7656036, ECO:0000269|PubMed:8450537,
FT ECO:0007744|PDB:1LLD, ECO:0007744|PDB:1LTH"
FT BINDING 126..129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000305|PubMed:7656036, ECO:0007744|PDB:1LTH"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 154..157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000305|PubMed:7656036, ECO:0007744|PDB:1LTH"
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:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|PubMed:7656036, ECO:0007744|PDB:1LTH"
FT BINDING 171..176
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:7656036,
FT ECO:0007744|PDB:1LTH"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000305|PubMed:7656036, ECO:0007744|PDB:1LTH"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 94..115
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1LTH"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 274..284
FT /evidence="ECO:0007829|PDB:1LLD"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1LLD"
FT HELIX 298..316
FT /evidence="ECO:0007829|PDB:1LLD"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:1LLD"
SQ SEQUENCE 320 AA; 34240 MW; D3E092AA9C353C4E CRC64;
MAETTVKPTK LAVIGAGAVG STLAFAAAQR GIAREIVLED IAKERVEAEV LDMQHGSSFY
PTVSIDGSDD PEICRDADMV VITAGPRQKP GQSRLELVGA TVNILKAIMP NLVKVAPNAI
YMLITNPVDI ATHVAQKLTG LPENQIFGSG TNLDSARLRF LIAQQTGVNV KNVHAYIAGE
HGDSEVPLWE SATIGGVPMC DWTPLPGHDP LDADKREEIH QEVKNAAYKI INGKGATNYA
IGMSGVDIIE AVLHDTNRIL PVSSMLKDFH GISDICMSVP TLLNRQGVNN TINTPVSDKE
LAALKRSAET LKETAAQFGF
