P99116 (LDHD_STAAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
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: D-lactate dehydrogenase Short name=D-LDH EC=1.1.1.28 Alternative name(s): D-specific D-2-hydroxyacid dehydrogenase | ||||||
| Gene names |
| ||||||
| Organism | Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 158879 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 330 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | (R)-lactate + NAD+ = pyruvate + NADH. |
| Sequence similarities | Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. |
| Sequence caution | The sequence BAB43615.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Molecular function | D-lactate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD 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 – 330 | 330 | D-lactate dehydrogenase | PRO_0000075961 | |||||
Regions | |||||||||
| Nucleotide binding | 156 – 157 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 233 – 235 | 3 | NAD By similarity | ||||||
| Nucleotide binding | 296 – 299 | 4 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 235 | 1 | By similarity | ||||||
| Active site | 264 | 1 | By similarity | ||||||
| Active site | 296 | 1 | Proton donor By similarity | ||||||
| Binding site | 259 | 1 | NAD By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315. |
| [2] | "Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315. |
| [3] | "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000018 Genomic DNA. Translation: BAB43615.1. Different initiation. |
| PIR | E90056. |
| RefSeq | NP_375636.1. NC_002745.2. |
3D structure databases | |
| ProteinModelPortal | P99116. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P99116. |
2D gel databases | |
| SWISS-2DPAGE | P99116. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000001918; EBSTAP00000001918; EBSTAG00000001918. |
| GeneID | 1125239. |
| GenomeReviews | Gene locus SA2312 in contig BA000018_GR. |
| KEGG | sau:SA2312. |
| PATRIC | 19577180. VBIStaAur116463_2508. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1052. |
| GeneTree | EBGT00050000024534. |
| HOGENOM | HBG731446. |
| ProtClustDB | PRK12480. |
Enzyme and pathway databases | |
| BioCyc | SAUR158879:SA2312-MONOMER. |
Family and domain databases | |
| InterPro | IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. |
| KO | K03778. |
| Pfam | PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view] |
| PROSITE | PS00065. D_2_HYDROXYACID_DH_1. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. 1 hit. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LDHD_STAAN | ||||||||
| Accession | Primary (citable) accession number: P99116 Secondary accession number(s): Q99RB1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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