(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 162.
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;
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};
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   SMR; P13714; -.
DR   STRING; 224308.BSU03050; -.
DR   iPTMnet; P13714; -.
DR   jPOST; P13714; -.
DR   PaxDb; P13714; -.
DR   PRIDE; P13714; -.
DR   EnsemblBacteria; CAB12099; CAB12099; BSU03050.
DR   GeneID; 938348; -.
DR   KEGG; bsu:BSU03050; -.
DR   PATRIC; fig|224308.43.peg.313; -.
DR   eggNOG; ENOG4105C80; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000213793; -.
DR   InParanoid; P13714; -.
DR   KO; K00016; -.
DR   OMA; MDLMQTA; -.
DR   BioCyc; BSUB:BSU03050-MONOMER; -.
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; 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;
DR   PRODOM; P13714.
DR   SWISS-2DPAGE; P13714.
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   NP_BIND         15..16
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:3PQD, ECO:0000244|PDB:3PQF,
FT                   ECO:0000269|Ref.7"
FT   NP_BIND         82..83
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:3PQF, ECO:0000255|HAMAP-
FT                   Rule:MF_00488, ECO:0000269|Ref.7"
FT   NP_BIND         121..123
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:3PQD, ECO:0000255|HAMAP-
FT                   Rule:MF_00488, ECO:0000305|Ref.7"
FT   REGION          123..126
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   REGION          151..154
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   REGION          168..172
FT                   /note="Allosteric activator binding"
FT                   /evidence="ECO:0000244|PDB:3PQD, ECO:0000269|Ref.7"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000244|PDB:3PQD, ECO:0000255|HAMAP-
FT                   Rule:MF_00488, ECO:0000305|Ref.7"
FT   BINDING         37
FT                   /note="NAD"
FT                   /evidence="ECO:0000244|PDB:3PQF, ECO:0000255|HAMAP-
FT                   Rule:MF_00488, ECO:0000269|Ref.7"
FT   BINDING         42
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         68
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         85
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         91
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         146
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT   BINDING         156
FT                   /note="Allosteric activator"
FT                   /evidence="ECO:0000244|PDB:3PQD, ECO:0000255|HAMAP-
FT                   Rule:MF_00488, ECO:0000269|Ref.7"
FT   BINDING         232
FT                   /note="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:0000244|PDB:3PQE"
FT   HELIX           15..27
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          31..36
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           40..52
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           54..56
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          57..59
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          62..66
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           68..71
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          75..79
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           91..111
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          116..120
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          122..124
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           125..136
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           140..142
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          143..145
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           149..160
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   TURN            161..164
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           167..169
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          174..179
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           186..188
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           196..201
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          204..206
FT                   /evidence="ECO:0000244|PDB:3PQF"
FT   HELIX           208..229
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           234..248
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          253..255
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          258..263
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           264..266
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          268..273
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          276..279
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   STRAND          282..286
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   HELIX           293..310
FT                   /evidence="ECO:0000244|PDB:3PQE"
FT   TURN            311..313
FT                   /evidence="ECO:0000244|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
//

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