LDH_BACSU
ID LDH_BACSU Reviewed; 320 AA.
AC P13714;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:3098260};
DE Short=L-LDH {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:3098260};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488};
GN Name=ldh {ECO:0000255|HAMAP-Rule:MF_00488};
GN Synonyms=lctE {ECO:0000303|PubMed:8969502}; OrderedLocusNames=BSU03050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 51 AND 57-58.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3098260; DOI=10.1515/bchm3.1986.367.2.891;
RA Hediger M.A., Frank G., Zuber H.;
RT "Structure and function of L-lactate dehydrogenases from thermophilic and
RT mesophilic bacteria, IV. The primary structure of the mesophilic lactate
RT dehydrogenase from Bacillus subtilis.";
RL Biol. Chem. Hoppe-Seyler 367:891-903(1986).
RN [5]
RP INDUCTION, AND PATHWAY.
RX PubMed=10809684; DOI=10.1128/jb.182.11.3072-3080.2000;
RA Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E.,
RA Dreesen O., Glaser P., Jahn D.;
RT "Fermentative metabolism of Bacillus subtilis: physiology and regulation of
RT gene expression.";
RL J. Bacteriol. 182:3072-3080(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD AND
RP FRUCTOSE-1-6-BISPHOSPHATE, ACTIVE SITE, AND SUBUNIT.
RA Zhang Y., Garavito R.M.;
RT "Crystal structure of L-lactate dehydrogenase from Bacillus subtilis
RT mutation H171C complexed with NAD+.";
RL Submitted (NOV-2010) to the PDB data bank.
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 ECO:0000305|PubMed:10809684}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00488,
CC ECO:0000305|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- INDUCTION: Strongly induced under anaerobic conditions. Activated by
CC ResDE, Fnr and ArfM. {ECO:0000269|PubMed:10809684}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08939.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB12099.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D50453; BAA08939.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12099.2; ALT_INIT; Genomic_DNA.
DR PIR; E69649; E69649.
DR RefSeq; NP_388187.2; NC_000964.3.
DR PDB; 3PQD; X-ray; 2.38 A; A/B/C/D/E/F/G/H=1-320.
DR PDB; 3PQE; X-ray; 2.20 A; A/B/C/D=1-320.
DR PDB; 3PQF; X-ray; 2.49 A; A/B/C/D=1-320.
DR PDBsum; 3PQD; -.
DR PDBsum; 3PQE; -.
DR PDBsum; 3PQF; -.
DR AlphaFoldDB; P13714; -.
DR SMR; P13714; -.
DR STRING; 224308.BSU03050; -.
DR iPTMnet; P13714; -.
DR jPOST; P13714; -.
DR PaxDb; P13714; -.
DR PRIDE; P13714; -.
DR EnsemblBacteria; CAB12099; CAB12099; BSU_03050.
DR GeneID; 938348; -.
DR KEGG; bsu:BSU03050; -.
DR PATRIC; fig|224308.43.peg.313; -.
DR eggNOG; COG0039; Bacteria.
DR InParanoid; P13714; -.
DR OMA; ASCAEYI; -.
DR BioCyc; BSUB:BSU03050-MON; -.
DR SABIO-RK; P13714; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
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; Direct protein sequencing; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..320
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000168329"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000305|Ref.7, ECO:0007744|PDB:3PQD"
FT BINDING 15..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD,
FT ECO:0007744|PDB:3PQF"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488,
FT ECO:0000269|Ref.7, ECO:0007744|PDB:3PQF"
FT BINDING 42
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 ECO:0000269|Ref.7, ECO:0007744|PDB:3PQF"
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 ECO:0000305|Ref.7, ECO:0007744|PDB:3PQD"
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 ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD"
FT BINDING 168..172
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:3PQD"
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 ECO:0000269|PubMed:17218307"
FT CONFLICT 38
FT /note="V -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="N -> P (in Ref. 1; BAA08939)"
FT /evidence="ECO:0000305"
FT CONFLICT 57..58
FT /note="AP -> GL (in Ref. 1; BAA08939)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="V -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="H -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..318
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 91..111
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:3PQE"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3PQF"
FT HELIX 208..229
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:3PQE"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3PQE"
FT HELIX 293..310
FT /evidence="ECO:0007829|PDB:3PQE"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:3PQE"
SQ SEQUENCE 320 AA; 34802 MW; F0B71F5A760FCAE1 CRC64;
MNKHVNKVAL IGAGFVGSSY AFALINQGIT DELVVIDVNK EKAMGDVMDL NHGKAFAPQP
VKTSYGTYED CKDADIVCIC AGANQKPGET RLELVEKNLK IFKGIVSEVM ASGFDGIFLV
ATNPVDILTY ATWKFSGLPK ERVIGSGTTL DSARFRFMLS EYFGAAPQNV HAHIIGEHGD
TELPVWSHAN VGGVPVSELV EKNDAYKQEE LDQIVDDVKN AAYHIIEKKG ATYYGVAMSL
ARITKAILHN ENSILTVSTY LDGQYGADDV YIGVPAVVNR GGIAGITELN LNEKEKEQFL
HSAGVLKNIL KPHFAEQKVN
