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RABIT:ALDOA
Contents
| Species (Taxon ID) | Oryctolagus cuniculus (Rabbit). (9986) | |
| Gene Name(s) | ALDOA | |
| Protein Name(s) | Fructose-bisphosphate aldolase A
Muscle-type aldolase | |
| External Links | ||
| UniProt | P00883 | |
| EMBL | K02300 V00876 V00877 | |
| PIR | A92444 | |
| RefSeq | NP_001075707.1 XP_008256151.1 XP_008256152.1 | |
| UniGene | Ocu.864 | |
| PDB | 1ADO 1EWD 1EWE 1EX5 1J4E 1ZAH 1ZAI 1ZAJ 1ZAL 2OT0 2OT1 2QUT 2QUU 2QUV 3B8D 3BV4 3DFN 3DFO 3DFP 3DFQ 3DFS 3DFT 3LGE 3TU9 6ALD | |
| PDBsum | 1ADO 1EWD 1EWE 1EX5 1J4E 1ZAH 1ZAI 1ZAJ 1ZAL 2OT0 2OT1 2QUT 2QUU 2QUV 3B8D 3BV4 3DFN 3DFO 3DFP 3DFQ 3DFS 3DFT 3LGE 3TU9 6ALD | |
| ProteinModelPortal | P00883 | |
| SMR | P00883 | |
| IntAct | P00883 | |
| MINT | MINT-7995296 | |
| STRING | 9986.ENSOCUP00000020204 | |
| BindingDB | P00883 | |
| ChEMBL | CHEMBL4695 | |
| PRIDE | P00883 | |
| Ensembl | ENSOCUT00000009869 | |
| GeneID | 100009055 | |
| CTD | 226 | |
| eggNOG | COG3588 | |
| GeneTree | ENSGT00390000010235 | |
| HOGENOM | HOG000220876 | |
| HOVERGEN | HBG002386 | |
| InParanoid | P00883 | |
| SABIO-RK | P00883 | |
| UniPathway | UPA00109 | |
| EvolutionaryTrace | P00883 | |
| Proteomes | UP000001811 | |
| GO | GO:0031674 GO:0031430 GO:0004332 GO:0006096 GO:0051289 | |
| Gene3D | 3.20.20.70 | |
| InterPro | IPR029768 IPR013785 IPR029769 IPR000741 | |
| PANTHER | PTHR11627 | |
| Pfam | PF00274 | |
| PROSITE | PS00158 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000315 |
F |
Table 1 shows the kinetics constants of wildtype Rabit Aldolase A reacting with fructose bisphosphate are much faster than those of mutated aldolase A. The "Kinetic Analysis" paragraph of materials and methods section say they used a glycerol-3-phosphate dehydrogen- ase/triose phosphate isomerase coupled assay, which would imply the formation of G3P, thus they show fructose bisphosphate aldolase activity. |
complete | |||||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0030335 |
positive regulation of cell migration |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0034316 |
negative regulation of Arp2/3 complex-mediated actin nucleation |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0051289 |
protein homotetramerization |
ECO:0000353 |
physical interaction evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0324 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0031674 |
I band |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0031430 |
M band |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Morris, AJ & Tolan, DR (1993) Site-directed mutagenesis identifies aspartate 33 as a previously unidentified critical residue in the catalytic mechanism of rabbit aldolase A. J. Biol. Chem. 268 1095-100 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Ritterson Lew, C & Tolan, DR (2013) Aldolase sequesters WASP and affects WASP/Arp2/3-stimulated actin dynamics. J. Cell. Biochem. 114 1928-39 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 Rangarajan, ES et al. (2010) Mechanism of aldolase control of sorting nexin 9 function in endocytosis. J. Biol. Chem. 285 11983-90 PubMed GONUTS page
