P44429 (ALF_HAEIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 87.
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 |
| ||||
| Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 71421 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › ![]() |
Protein attributes
| Sequence length | 359 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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. |
| Catalytic activity | D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. |
| Cofactor | Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity. |
| Pathway | |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the class II fructose-bisphosphate aldolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 359 | 359 | Fructose-bisphosphate aldolase | PRO_0000178716 | |||||
Regions | |||||||||
| Region | 266 – 268 | 3 | Dihydroxyacetone phosphate binding By similarity | ||||||
| Region | 287 – 290 | 4 | Dihydroxyacetone phosphate binding By similarity | ||||||
Sites | |||||||||
| Active site | 110 | 1 | Proton donor By similarity | ||||||
| Metal binding | 111 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 145 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 175 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 227 | 1 | Zinc 1; catalytic By similarity | ||||||
| Metal binding | 265 | 1 | Zinc 1; catalytic By similarity | ||||||
| Binding site | 62 | 1 | Glyceraldehyde 3-phosphate By similarity | ||||||
| Binding site | 228 | 1 | Dihydroxyacetone phosphate; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L42023 Genomic DNA. Translation: AAC22182.1. |
| PIR | C64074. |
| RefSeq | NP_438682.1. NC_000907.1. |
3D structure databases | |
| ProteinModelPortal | P44429. |
| SMR | P44429. Positions 2-359. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 71421.HI0524. |
Proteomic databases | |
| PRIDE | P44429. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC22182; AAC22182; HI_0524. |
| GeneID | 949539. |
| KEGG | hin:HI0524. |
| PATRIC | 20189601. VBIHaeInf48452_0543. |
Phylogenomic databases | |
| eggNOG | COG0191. |
| KO | K01624. |
| OMA | REGEKTM. |
| ProtClustDB | PRK09197. |
Enzyme and pathway databases | |
| UniPathway | UPA00109; UER00183. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| InterPro | IPR013785. Aldolase_TIM. IPR006411. Fruct_bisP_bact. 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. TIGR01520. FruBisAldo_II_A. 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_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P44429 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
