Reviewed,
UniProtKB/Swiss-Prot Q6GDK1 (LDH2_STAAR)
Last modified
November 25, 2008.
Version 37.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: L-lactate dehydrogenase 2 Short name=L-LDH 2 EC=1.1.1.27 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 282458 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 319 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Contributes to S.aureus growth during nitrosative stress in both aerobically and anaerobically cultured cells, despite playing a secondary role in this resistance mechanism By similarity. |
| Catalytic activity | (S)-lactate + NAD(+) = pyruvate + NADH. |
| Pathway | Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | CytoplasmBy similarity. |
| Sequence similarities | Belongs to the LDH/MDH superfamily. LDH family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Glycolysis Stress response |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | anaerobic glycolysis Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW response to stressInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: HAMAP |
| Molecular function | L-lactate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 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 – 319 | 319 | L-lactate dehydrogenase 2 | PRO_0000168384 | |||||
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 | 231 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 222 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| BX571856 Genomic DNA. Translation: CAG41657.1. | |
| RefSeq | YP_042022.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2859696. |
| GenomeReviews | Gene locus SAR2680 in contig BX571856_GR. |
| KEGG | sar:SAR2680. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q6GDK1. |
Enzyme and pathway databases | |
| BioCyc | SAUR282458:SAR2680-MON. |
Family and domain databases | |
| HAMAP | MF_00488. [Tree] |
| InterPro | IPR001557. L-lactate/malate_DHase. IPR011304. L-lactate_DHase. IPR001236. Lactate/malate_DHase. IPR015955. Lactate_DHase/Glyco_Ohase_4_C. IPR016040. NAD(P)-bd. [Graphical view] |
| Gene3D | G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 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. |
| TIGRFAMs | TIGR01771. L-LDH-NAD. 1 hit. |
| PROSITE | PS00064. L_LDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LDH2_STAAR | ||||||||
| Accession | Primary (citable) accession number: Q6GDK1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


