D5HB48 (D5HB48_SALRM) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 20.
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-phosphofructokinase HAMAP-Rule MF_00339 Short name=Phosphofructokinase HAMAP-Rule MF_00339 EC=2.7.1.11 HAMAP-Rule MF_00339 Alternative name(s): Phosphohexokinase HAMAP-Rule MF_00339 | ||||
| Gene names |
| ||||
| Organism | Salinibacter ruber (strain M8) [Complete proteome] [HAMAP] EMBL CBH25253.1 | ||||
| Taxonomic identifier | 761659 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Salinibacter › ![]() |
Protein attributes
| Sequence length | 379 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339 SAAS SAAS000023 |
| Pathway | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339 SAAS SAAS000023 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00339. |
| Sequence similarities | Belongs to the phosphofructokinase family. HAMAP-Rule MF_00339 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis HAMAP-Rule MF_00339 SAAS SAAS000023 |
| Cellular component | Cytoplasm HAMAP-Rule MF_00339 SAAS SAAS000023 |
| Ligand | ATP-binding RuleBase RU004092 HAMAP-Rule MF_00339 SAAS SAAS015912 Magnesium HAMAP-Rule MF_00339 Metal-binding HAMAP-Rule MF_00339 Nucleotide-binding |
| Molecular function | Kinase RuleBase RU004092 HAMAP-Rule MF_00339 SAAS SAAS015912 EMBL CBH25253.1 Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | fructose 6-phosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysisInferred from electronic annotation. Source: HAMAP |
| Cellular_component | 6-phosphofructokinase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | 6-phosphofructokinase activity Inferred from electronic annotation. Source: HAMAP ATP bindingInferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 25 – 29 | 5 | ATP By similarity HAMAP-Rule MF_00339 | ||||||
| Nucleotide binding | 165 – 169 | 5 | ATP By similarity HAMAP-Rule MF_00339 | ||||||
| Nucleotide binding | 182 – 198 | 17 | ATP By similarity HAMAP-Rule MF_00339 | ||||||
Sites | |||||||||
| Active site | 138 | 1 | Proton acceptor By similarity HAMAP-Rule MF_00339 | ||||||
| Metal binding | 196 | 1 | Magnesium; via carbonyl oxygen By similarity HAMAP-Rule MF_00339 | ||||||
| Metal binding | 198 | 1 | Magnesium By similarity HAMAP-Rule MF_00339 | ||||||
| Binding site | 173 | 1 | Substrate By similarity HAMAP-Rule MF_00339 | ||||||
| Binding site | 277 | 1 | Substrate By similarity HAMAP-Rule MF_00339 | ||||||
| Binding site | 283 | 1 | Substrate By similarity HAMAP-Rule MF_00339 | ||||||
| Binding site | 286 | 1 | Substrate By similarity HAMAP-Rule MF_00339 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Fine-scale evolution: genomic, phenotypic and ecological differentiation in two coexisting Salinibacter ruber strains." Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P., Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I., Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R., Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J. ISME J. -:0-0(2010) Cited for: NUCLEOTIDE SEQUENCE. Strain: M8. |
| [2] | "Genome sequence of Salinibacter ruber M8." Genoscope Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: M8. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FP565814 Genomic DNA. Translation: CBH25253.1. |
| RefSeq | YP_003572205.1. NC_014032.1. |
3D structure databases | |
| ProteinModelPortal | D5HB48. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | D5HB48. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CBH25253; CBH25253; SRM_02332. |
| GeneID | 8995079. |
| KEGG | srm:SRM_02332. |
| PATRIC | 35492548. VBISalRub49863_2254. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000248869. |
| KO | K00850. |
| PhylomeDB | D5HB48. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00182. |
Family and domain databases | |
| HAMAP | MF_00339. Phosphofructokinase. |
| InterPro | IPR012003. ATP_PFK_prok. IPR022953. Phosphofructokinase. IPR015912. Phosphofructokinase_CS. IPR000023. Phosphofructokinase_dom. [Graphical view] |
| Pfam | PF00365. PFK. 1 hit. [Graphical view] |
| PIRSF | PIRSF000532. ATP_PFK_prok. 1 hit. |
| PRINTS | PR00476. PHFRCTKINASE. |
| SUPFAM | SSF53784. Ppfruckinase. 1 hit. |
| PROSITE | PS00433. PHOSPHOFRUCTOKINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | D5HB48_SALRM | ||||||||
| Accession | Primary (citable) accession number: D5HB48 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
