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RABIT:ALDOA

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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

PMID:8419316[1]

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
CACAO 5675

enables

GO:0004332

fructose-bisphosphate aldolase activity

PMID:23495010[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0030335

positive regulation of cell migration

PMID:23495010[2]

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

PMID:23495010[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

PMID:8419316[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0051289

protein homotetramerization

PMID:20129922[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P00883

P

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:20129922[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

PMID:20129922[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013785

F

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000741

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000741

P

Seeded From UniProt

complete

enables

GO:0004332

fructose-bisphosphate aldolase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.2.13

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0324
UniPathway:UPA00109

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

part_of

GO:0031674

I band

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0478

C

Seeded From UniProt

complete

part_of

GO:0031430

M band

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0315

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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. 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. 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