D0K592 (D0K592_STAAD) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 21.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: 6-phosphogluconate dehydrogenase, decarboxylating PIRNR PIRNR000109 RuleBase RU000485 EC=1.1.1.44 PIRNR PIRNR000109 RuleBase RU000485 | ||
| Gene names |
| ||
| Organism | Staphylococcus aureus (strain ED98) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 681288 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 468 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH By similarity. PIRNR PIRNR000109 |
| Catalytic activity | 6-phospho-D-gluconate + NADP+ = D-ribulose 5-phosphate + CO2 + NADPH. PIRNR PIRNR000109 RuleBase RU000485 |
| Pathway | Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 3/3. PIRNR PIRNR000109 RuleBase RU004281 |
| Subunit structure | Homodimer By similarity. PIRNR PIRNR000109 |
| Sequence similarities | Belongs to the 6-phosphogluconate dehydrogenase family. PIRNR PIRNR000109 RuleBase RU000485 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconate utilization RuleBase RU000486 Pentose shunt PIRNR PIRNR000109 RuleBase RU004281 |
| Ligand | NADP PIRNR PIRNR000109 RuleBase RU000485 |
| Molecular function | Oxidoreductase PIRNR PIRNR000109 RuleBase RU000485 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | D-gluconate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shuntInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NADP binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 9 – 14 | 6 | NADP By similarity PIRSR PIRSR000109-3 | ||||||
| Nucleotide binding | 32 – 34 | 3 | NADP By similarity PIRSR PIRSR000109-3 | ||||||
| Nucleotide binding | 73 – 75 | 3 | NADP By similarity PIRSR PIRSR000109-3 | ||||||
| Region | 127 – 129 | 3 | Substrate binding By similarity PIRSR PIRSR000109-2 | ||||||
| Region | 185 – 186 | 2 | Substrate binding By similarity PIRSR PIRSR000109-2 | ||||||
Sites | |||||||||
| Active site | 182 | 1 | Proton acceptor By similarity PIRSR PIRSR000109-1 | ||||||
| Active site | 189 | 1 | Proton donor By similarity PIRSR PIRSR000109-1 | ||||||
| Binding site | 101 | 1 | NADP By similarity PIRSR PIRSR000109-3 | ||||||
| Binding site | 101 | 1 | Substrate By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 190 | 1 | Substrate By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 259 | 1 | Substrate; via amide nitrogen By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 286 | 1 | Substrate By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 444 | 1 | Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 450 | 1 | Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2 | ||||||
Sequences
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References
| [1] | "Recent human-to-poultry host jump, adaptation, and pandemic spread of Staphylococcus aureus." Lowder B.V., Guinane C.M., Ben Zakour N.L., Weinert L.A., Conway-Morris A., Cartwright R.A., Simpson A.J., Rambaut A., Nubel U., Fitzgerald J.R. Proc. Natl. Acad. Sci. U.S.A. 106:19545-19550(2009) [PubMed: 19884497] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001781 Genomic DNA. Translation: ACY11402.1. |
| RefSeq | YP_003282408.1. NC_013450.1. |
3D structure databases | |
| ProteinModelPortal | D0K592. |
| SMR | D0K592. Positions 6-465. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | D0K592. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000055162; EBSTAP00000053724; EBSTAG00000057637. |
| GeneID | 8614247. |
| GenomeReviews | Gene locus SAAV_1502 in contig CP001781_GR. |
| KEGG | sad:SAAV_1502. |
| PATRIC | 32447051. VBIStaAur139507_1500. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000025238. |
| OMA | SNYPDTN. |
Family and domain databases | |
| InterPro | IPR008927. 6-PGluconate_DH_C-like. IPR006114. 6PGDH_C. IPR006113. 6PGDH_decarbox. IPR006115. 6PGDH_NADP-bd. IPR006184. 6PGdom_BS. IPR013328. DH_multihelical. IPR012284. Fibritin/6PGD_C-extension. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:1.20.5.320. Fibritin/6PGD_C-extension. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit. |
| KO | K00033. |
| Pfam | PF00393. 6PGD. 1 hit. PF03446. NAD_binding_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000109. 6PGD. 1 hit. |
| SUPFAM | SSF48179. 6DGDH_C_like. 1 hit. |
| TIGRFAMs | TIGR00873. Gnd. 1 hit. |
| PROSITE | PS00461. 6PGD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | D0K592_STAAD | ||||||||
| Accession | Primary (citable) accession number: D0K592 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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