P13714 (LDH_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 109.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: L-lactate dehydrogenase Short name=L-LDH EC=1.1.1.27 | ||||||
| Gene names |
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| Organism | Bacillus subtilis | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 320 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | (S)-lactate + NAD+ = pyruvate + NADH. HAMAP MF_00488 |
| Pathway | Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP MF_00488 |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Induction | Strongly induced under anaerobic conditions. Activated by ResDE, Fnr and ArfM. Ref.5 |
| Sequence similarities | Belongs to the LDH/MDH superfamily. LDH family. |
| Sequence caution | The sequence BAA08939.1 differs from that shown. Reason: Erroneous initiation. The sequence CAB12099.2 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | L-lactate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 320 | 320 | L-lactate dehydrogenase HAMAP MF_00488 | PRO_0000168329 | |||||
Regions | |||||||||
| Nucleotide binding | 14 – 42 | 29 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 178 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 91 | 1 | Substrate By similarity | ||||||
| Binding site | 123 | 1 | NAD or substrate By similarity | ||||||
| Binding site | 154 | 1 | Substrate By similarity | ||||||
| Binding site | 232 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 223 | 1 | Phosphotyrosine Ref.6 | ||||||
Experimental info | |||||||||
| Sequence conflict | 38 | 1 | V → L AA sequence Ref.4 | ||||||
| Sequence conflict | 51 | 1 | N → P in BAA08939. Ref.1 | ||||||
| Sequence conflict | 57 – 58 | 2 | AP → GL in BAA08939. Ref.1 | ||||||
| Sequence conflict | 120 | 1 | V → I AA sequence Ref.4 | ||||||
| Sequence conflict | 224 | 1 | H → T AA sequence Ref.4 | ||||||
| Sequence conflict | 315 – 318 | 4 | Missing AA sequence Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes." Yamane K., Kumano M., Kurita K. Microbiology 142:3047-3056(1996) [PubMed: 8969502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 51 AND 57-58. |
| [4] | "Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, IV. The primary structure of the mesophilic lactate dehydrogenase from Bacillus subtilis." Hediger M.A., Frank G., Zuber H. Biol. Chem. Hoppe-Seyler 367:891-903(1986) [PubMed: 3098260] [Abstract] Cited for: PROTEIN SEQUENCE. |
| [5] | "Fermentative metabolism of Bacillus subtilis: physiology and regulation of gene expression." Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E., Dreesen O., Glaser P., Jahn D. J. Bacteriol. 182:3072-3080(2000) [PubMed: 10809684] [Abstract] Cited for: REGULATION. |
| [6] | "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed: 17218307] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, MASS SPECTROMETRY. Strain: 168. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D50453 Genomic DNA. Translation: BAA08939.1. Different initiation. AL009126 Genomic DNA. Translation: CAB12099.2. Different initiation. |
| PIR | E69649. |
| RefSeq | NP_388187.2. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P13714. |
| SMR | P13714. Positions 7-314. |
| ModBase | Search... |
PTM databases | |
| PhosSite | P13714. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000003920; EBBACP00000003920; EBBACG00000003912. |
| GeneID | 938348. |
| GenomeReviews | Gene locus BSU03050 in contig AL009126_GR. |
| KEGG | bsu:BSU03050. |
| NMPDR | fig|224308.1.peg.306. |
| PATRIC | 18972169. VBIBacSub10457_0313. |
Organism-specific databases | |
| GenoList | BSU03050. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00050000001153. |
| HOGENOM | HBG566126. |
| PhylomeDB | P13714. |
| ProtClustDB | PRK00066. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU03050-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00488. Lactate_dehydrog. [Tree] |
| InterPro | IPR001557. L-lactate/malate_DH. IPR011304. L-lactate_DH. IPR018177. L-lactate_DH_AS. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00016. |
| PANTHER | PTHR11540:SF3. PTHR11540:SF3. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000102. Lac_mal_DH. 1 hit. |
| PRINTS | PR00086. LLDHDRGNASE. |
| SUPFAM | SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
| TIGRFAMs | TIGR01771. L-LDH-NAD. 1 hit. |
| PROSITE | PS00064. L_LDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LDH_BACSU | ||||||||
| Accession | Primary (citable) accession number: P13714 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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