Q8YNK2 (ALF_NOSS1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 69.
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: Fructose-bisphosphate aldolase Short name=FBP aldolase Short name=FBPA EC=4.1.2.13 Alternative name(s): Fructose-1,6-bisphosphate aldolase | ||||
| Gene names |
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| Organism | Nostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 103690 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc![]() |
Protein attributes
| Sequence length | 359 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis By similarity. UniProtKB Q55664 |
| Catalytic activity | D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. UniProtKB Q55664 |
| Cofactor | Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity. UniProtKB Q55664 |
| Pathway | Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. UniProtKB Q55664 |
| Sequence similarities | Belongs to the class II fructose-bisphosphate aldolase family. |
| Mass spectrometry | Molecular mass is 38764±1 Da from positions 1 - 359. Determined by MALDI. Ref.2 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity UniProtKB Q55664 | ||||||
| Chain | 2 – 359 | 358 | Fructose-bisphosphate aldolase UniProtKB Q55664 | PRO_0000366199 | |||||
Regions | |||||||||
| Region | 233 – 235 | 3 | Dihydroxyacetone phosphate binding By similarity UniProtKB Q55664 | ||||||
| Region | 275 – 278 | 4 | Dihydroxyacetone phosphate binding By similarity UniProtKB Q55664 | ||||||
Sites | |||||||||
| Active site | 83 | 1 | Proton donor By similarity UniProtKB Q55664 | ||||||
| Metal binding | 84 | 1 | Zinc 1; catalytic By similarity UniProtKB Q55664 | ||||||
| Metal binding | 105 | 1 | Zinc 2 By similarity UniProtKB Q55664 | ||||||
| Metal binding | 142 | 1 | Zinc 2 By similarity UniProtKB Q55664 | ||||||
| Metal binding | 198 | 1 | Zinc 1; catalytic By similarity UniProtKB Q55664 | ||||||
| Metal binding | 232 | 1 | Zinc 1; catalytic By similarity UniProtKB Q55664 | ||||||
| Binding site | 50 | 1 | Glyceraldehyde 3-phosphate By similarity UniProtKB Q55664 | ||||||
| Binding site | 199 | 1 | Dihydroxyacetone phosphate; via amide nitrogen By similarity UniProtKB Q55664 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. Tabata S.DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 7120 / UTEX 2576. |
| [2] | Singh H., Rajaram H., Apte S.K. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 282-289, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000019 Genomic DNA. Translation: BAB76262.1. |
| PIR | AC2376. |
| RefSeq | NP_488603.1. NC_003272.1. |
3D structure databases | |
| ProteinModelPortal | Q8YNK2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 103690.all4563. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB76262; BAB76262; BAB76262. |
| GeneID | 1108164. |
| KEGG | ana:all4563. |
| PATRIC | 22779738. VBINosSp37423_5315. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0191. |
| HOGENOM | HOG000227792. |
| KO | K01624. |
| OMA | VNAPVIM. |
| ProtClustDB | PRK09196. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00183. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| InterPro | IPR013785. Aldolase_TIM. IPR006412. Fruct_bisP_Calv. IPR000771. Ketose_bisP_aldolase_II. [Graphical view] |
| Pfam | PF01116. F_bP_aldolase. 1 hit. [Graphical view] |
| PIRSF | PIRSF001359. F_bP_aldolase_II. 1 hit. |
| TIGRFAMs | TIGR00167. cbbA. 1 hit. TIGR01521. FruBisAldo_II_B. 1 hit. |
| PROSITE | PS00602. ALDOLASE_CLASS_II_1. 1 hit. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ALF_NOSS1 | ||||||||
| Accession | Primary (citable) accession number: Q8YNK2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
