C5Q9D1 (C5Q9D1_STAEP) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 17.
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 epidermidis BCM-HMP0060 EMBL EES58261.1 | ||||
| Taxonomic identifier | 525374 [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 EMBL EES58261.1 |
| 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] | Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y. Gibbs R.Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: BCM-HMP0060 EMBL EES58261.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ACHE01000041 Genomic DNA. Translation: EES58261.1. |
3D structure databases | |
| ProteinModelPortal | C5Q9D1. |
| SMR | C5Q9D1. Positions 6-465. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 31392750. VBIStaEpi34063_1536. |
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. |
| 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 | C5Q9D1_STAEP | ||||||||
| Accession | Primary (citable) accession number: C5Q9D1 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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