Q6GCN4 (LDH1_STAAS) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 61.
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 1 Short name=L-LDH 1 EC=1.1.1.27 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 282459 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 317 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Appears to be the primary factor that allows S.aureus growth during nitrosative stress in both aerobically and anaerobically cultured cells By similarity. HAMAP MF_00488 |
| 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 By similarity. HAMAP MF_00488 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00488. |
| 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 | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW response to stressInferred 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 – 317 | 317 | L-lactate dehydrogenase 1 HAMAP MF_00488 | PRO_0000168385 | |||||
Regions | |||||||||
| Nucleotide binding | 15 – 43 | 29 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 179 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 92 | 1 | Substrate By similarity | ||||||
| Binding site | 124 | 1 | NAD or substrate By similarity | ||||||
| Binding site | 155 | 1 | Substrate By similarity | ||||||
| Binding site | 232 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 223 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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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]. Strain: MSSA476. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX571857 Genomic DNA. Translation: CAG41985.1. |
| RefSeq | YP_042339.1. NC_002953.3. |
3D structure databases | |
| ProteinModelPortal | Q6GCN4. |
| SMR | Q6GCN4. Positions 1-313. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6GCN4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000024114; EBSTAP00000023281; EBSTAG00000024113. |
| GeneID | 2864185. |
| GenomeReviews | Gene locus SAS0217 in contig BX571857_GR. |
| KEGG | sas:SAS0217. |
| PATRIC | 19549780. VBIStaAur96780_0228. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0039. |
| GeneTree | EBGT00050000024431. |
| HOGENOM | HBG566126. |
| OMA | MDLNHGV. |
| PhylomeDB | Q6GCN4. |
| ProtClustDB | CLSK884508. |
Enzyme and pathway databases | |
| BioCyc | SAUR282459:SAS0217-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 | LDH1_STAAS | ||||||||
| Accession | Primary (citable) accession number: Q6GCN4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with