Q2JIY1 (Q2JIY1_SYNJB) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 62.
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 | Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP] EMBL ABD03413.1 | ||||
| Taxonomic identifier | 321332 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus![]() |
Protein attributes
| Sequence length | 472 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 RU000485 |
| 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 RU000485 |
| Ligand | NADP PIRNR PIRNR000109 RuleBase RU000485 |
| Molecular function | Oxidoreductase PIRNR PIRNR000109 RuleBase RU000485 EMBL ABD03413.1 |
| 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-UniPathway |
| 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 | 10 – 15 | 6 | NADP By similarity PIRSR PIRSR000109-3 | ||||||
| Nucleotide binding | 33 – 35 | 3 | NADP By similarity PIRSR PIRSR000109-3 | ||||||
| Nucleotide binding | 75 – 77 | 3 | NADP By similarity PIRSR PIRSR000109-3 | ||||||
| Region | 129 – 131 | 3 | Substrate binding By similarity PIRSR PIRSR000109-2 | ||||||
| Region | 186 – 187 | 2 | Substrate binding By similarity PIRSR PIRSR000109-2 | ||||||
Sites | |||||||||
| Active site | 183 | 1 | Proton acceptor By similarity PIRSR PIRSR000109-1 | ||||||
| Active site | 190 | 1 | Proton donor By similarity PIRSR PIRSR000109-1 | ||||||
| Binding site | 103 | 1 | NADP By similarity PIRSR PIRSR000109-3 | ||||||
| Binding site | 103 | 1 | Substrate By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 191 | 1 | Substrate By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 261 | 1 | Substrate; via amide nitrogen By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 288 | 1 | Substrate By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 446 | 1 | Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2 | ||||||
| Binding site | 452 | 1 | Substrate; shared with dimeric partner By similarity PIRSR PIRSR000109-2 | ||||||
Sequences
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References
| [1] | "Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses." Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F. ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JA-2-3B'a(2-13). |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000240 Genomic DNA. Translation: ABD03413.1. |
| RefSeq | YP_478676.1. NC_007776.1. |
3D structure databases | |
| ProteinModelPortal | Q2JIY1. |
| SMR | Q2JIY1. Positions 1-468. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 321332.CYB_2481. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABD03413; ABD03413; CYB_2481. |
| GeneID | 3902474. |
| KEGG | cyb:CYB_2481. |
| PATRIC | 23807312. VBISynSp29577_2481. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0362. |
| HOGENOM | HOG000255147. |
| KO | K00033. |
| OMA | KQQIGVI. |
| ProtClustDB | CLSK750283. |
Enzyme and pathway databases | |
| UniPathway | UPA00115; UER00410. |
Family and domain databases | |
| Gene3D | 1.10.1040.10. 1 hit. 1.20.5.320. 1 hit. 3.40.50.720. 1 hit. |
| 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] |
| 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 | Q2JIY1_SYNJB | ||||||||
| Accession | Primary (citable) accession number: Q2JIY1 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
