| IED ID | IndEnz0002019345 |
| Enzyme Type ID | protease019345 |
| Protein Name |
Fructose-bisphosphate aldolase A EC 4.1.2.13 Aldolase 1 Muscle-type aldolase |
| Gene Name | Aldoa Aldo1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MPHPYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYIKRALANSLACQGKYTPSGQSGAAASESLFISNHAY |
| Enzyme Length | 364 |
| Uniprot Accession Number | P05064 |
| Absorption | |
| Active Site | ACT_SITE 188; /note=Proton acceptor; /evidence=ECO:0000250; ACT_SITE 230; /note=Schiff-base intermediate with dihydroxyacetone-P |
| Activity Regulation | |
| Binding Site | BINDING 56; /note=Substrate; BINDING 147; /note=Substrate |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; |
| DNA Binding | |
| EC Number | 4.1.2.13 |
| Enzyme Function | FUNCTION: Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. |
| nucleotide Binding | |
| Features | Active site (2); Binding site (2); Chain (1); Cross-link (2); Initiator methionine (1); Modified residue (15); Sequence conflict (1); Site (1) |
| Keywords | Acetylation;Cytoplasm;Direct protein sequencing;Glycolysis;Hydroxylation;Isopeptide bond;Lyase;Phosphoprotein;Reference proteome;Schiff base;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band. Cytoplasm, myofibril, sarcomere, M line. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+). {ECO:0000250}. |
| Modified Residue | MOD_RES 5; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:P05065; MOD_RES 9; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 36; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 39; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 42; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 46; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 99; /note=N6-(2-hydroxyisobutyryl)lysine; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 108; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 111; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P09972; MOD_RES 111; /note=N6-malonyllysine; alternate; /evidence=ECO:0000250; MOD_RES 132; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05065; MOD_RES 147; /note=N6-(2-hydroxyisobutyryl)lysine; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 272; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04075; MOD_RES 312; /note=N6-malonyllysine; /evidence=ECO:0000250; MOD_RES 330; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P04075 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 11785984; 12466851; 12904583; 1383034; 14610273; 14630798; 14681479; 15102471; 15485910; 15627969; 15741177; 16141072; 16602821; 16615898; 16635246; 16687649; 1728594; 17500595; 17626619; 17634366; 17659271; 18614564; 18676612; 18698006; 18799693; 19423573; 19562802; 19723774; 20185832; 20697350; 21267068; 21278135; 21677750; 21884692; 23263557; 23495010; 23886627; 24006456; 24194600; 24390569; 24852826; 25196998; 25340332; 25637246; 26697723; 27173853; 27215380; 27597886; 28049690; 28245920; 30733279; 33059001; 34127677; 9395505; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,356 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:14729 |
| Cross Reference Brenda |