UniProtKB - P00883 (ALDOA_RABIT)
Protein
Fructose-bisphosphate aldolase A
Gene
ALDOA
Organism
Oryctolagus cuniculus (Rabbit)
Status
Functioni
Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.1 Publication
Miscellaneous
In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.
Alkylation of Arg-43 inactivates the enzyme.
Catalytic activityi
- β-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate1 PublicationEC:4.1.2.131 Publication
: glycolysis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.Proteins known to be involved in the 4 steps of the subpathway in this organism are:
- Hexokinase (HK1), Hexokinase (HK2), Hexokinase (HKDC1), Hexokinase (HK3), Hexokinase (HK2), Hexokinase (HK1), Hexokinase (HK3), Hexokinase (HK2), Hexokinase (HK3)
- Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI)
- ATP-dependent 6-phosphofructokinase (PFKM), PFK domain-containing protein, ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKM)
- Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 43 | SubstrateCombined sources1 Publication | 1 | |
Sitei | 73 | Essential for substrate cleavage | 1 | |
Sitei | 108 | Essential for substrate cleavage | 1 | |
Sitei | 147 | Alkylation inactivates the enzyme | 1 | |
Active sitei | 188 | Proton acceptor1 Publication | 1 | |
Active sitei | 230 | Schiff-base intermediate with dihydroxyacetone-P1 Publication | 1 | |
Binding sitei | 304 | SubstrateCombined sources1 Publication | 1 | |
Sitei | 362 | Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base | 1 | |
Sitei | 364 | Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate | 1 |
GO - Molecular functioni
- fructose-bisphosphate aldolase activity Source: UniProtKB
GO - Biological processi
- glycolytic process Source: UniProtKB
- negative regulation of Arp2/3 complex-mediated actin nucleation Source: CAFA
- positive regulation of cell migration Source: CAFA
- protein homotetramerization Source: UniProtKB
Keywordsi
Molecular function | Lyase |
Biological process | Glycolysis |
Ligand | Schiff base |
Enzyme and pathway databases
BRENDAi | 4.1.2.13, 1749 |
SABIO-RKi | P00883 |
UniPathwayi | UPA00109;UER00183 |
Protein family/group databases
MoonProti | P00883 |
Names & Taxonomyi
Protein namesi | Recommended name: Fructose-bisphosphate aldolase A (EC:4.1.2.13)Alternative name(s): Muscle-type aldolase |
Gene namesi | Name:ALDOA |
Organismi | Oryctolagus cuniculus (Rabbit) |
Taxonomic identifieri | 9986 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 35 | E → A: Reduces activity 14-fold. 1 Publication | 1 | |
Mutagenesisi | 43 | R → A: Reduces activity 14-fold. 1 Publication | 1 | |
Mutagenesisi | 129 | D → V: Alters protein-protein interactions, leading to a dimeric protein. | 1 | |
Mutagenesisi | 147 | K → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 188 | E → A: Reduces activity over 100-fold. 1 Publication | 1 | |
Mutagenesisi | 188 | E → Q: Reduces activity over 1000-fold. 1 Publication | 1 | |
Mutagenesisi | 190 | E → Q: Reduces activity 20-fold. 1 Publication | 1 | |
Mutagenesisi | 230 | K → M: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 304 | R → A: Reduces activity 400-fold. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4695 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000216938 | 2 – 364 | Fructose-bisphosphate aldolase AAdd BLAST | 363 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 9 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 36 | PhosphoserineBy similarity | 1 | |
Modified residuei | 39 | PhosphoserineBy similarity | 1 | |
Modified residuei | 42 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 42 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity | ||
Cross-linki | 42 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 46 | PhosphoserineBy similarity | 1 | |
Modified residuei | 99 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 108 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 111 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 111 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 132 | PhosphoserineBy similarity | 1 | |
Modified residuei | 272 | PhosphoserineBy similarity | 1 | |
Modified residuei | 312 | N6-malonyllysineBy similarity | 1 | |
Modified residuei | 330 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 361 | Deamidated asparagine; in form beta1 Publication | 1 |
Post-translational modificationi
Asn-361 in form alpha is deaminated to Asp in form beta.
Keywords - PTMi
Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PRIDEi | P00883 |
PTM databases
iPTMneti | P00883 |
MetOSitei | P00883 |
Expressioni
Gene expression databases
Bgeei | ENSOCUG00000006329, Expressed in smooth muscle tissue and 17 other tissues |
Interactioni
Subunit structurei
Homotetramer.
Interacts with SNX9 and WAS.
Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+.
6 PublicationsProtein-protein interaction databases
BioGRIDi | 1172078, 2 interactors |
IntActi | P00883, 1 interactor |
MINTi | P00883 |
STRINGi | 9986.ENSOCUP00000008499 |
Chemistry databases
BindingDBi | P00883 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
PCDDBi | P00883 |
SASBDBi | P00883 |
SMRi | P00883 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P00883 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 272 – 274 | Substrate bindingCombined sources1 Publication | 3 |
Sequence similaritiesi
Belongs to the class I fructose-bisphosphate aldolase family.Curated
Phylogenomic databases
eggNOGi | KOG1557, Eukaryota |
GeneTreei | ENSGT00950000182987 |
HOGENOMi | CLU_031243_1_0_1 |
InParanoidi | P00883 |
OMAi | DYREMLF |
OrthoDBi | 799973at2759 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
InterProi | View protein in InterPro IPR029768, Aldolase_I_AS IPR013785, Aldolase_TIM IPR000741, FBA_I |
Pfami | View protein in Pfam PF00274, Glycolytic, 1 hit |
PROSITEi | View protein in PROSITE PS00158, ALDOLASE_CLASS_I, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
P00883-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPHSHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE
60 70 80 90 100
NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS
110 120 130 140 150
KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKYSHEEIA
260 270 280 290 300
MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
310 320 330 340 350
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG
360
AAASESLFIS NHAY
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A5F9D5U7 | A0A5F9D5U7_RABIT | Fructose-bisphosphate aldolase | 419 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 35 | E → Q AA sequence (PubMed:1122141).Curated | 1 | |
Sequence conflicti | 274 – 276 | GQS → SQE AA sequence (PubMed:1122142).Curated | 3 | |
Sequence conflicti | 276 | S → E AA sequence (PubMed:1122142).Curated | 1 | |
Sequence conflicti | 294 – 296 | KPW → WPK AA sequence (PubMed:1122142).Curated | 3 | |
Sequence conflicti | 354 | S → R in CAA24246 (PubMed:6687628).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K02300 mRNA Translation: AAA31156.1 V00876 mRNA Translation: CAA24245.1 V00877 mRNA Translation: CAA24246.1 |
PIRi | A92444, ADRBA |
RefSeqi | NP_001075707.1, NM_001082238.1 XP_008256151.1, XM_008257929.2 XP_008256152.1, XM_008257930.2 XP_017197924.1, XM_017342435.1 |
Genome annotation databases
Ensembli | ENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329 |
GeneIDi | 100009055 |
KEGGi | ocu:100009055 |
Similar proteinsi
Cross-referencesi
Web resourcesi
Worthington enzyme manual |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K02300 mRNA Translation: AAA31156.1 V00876 mRNA Translation: CAA24245.1 V00877 mRNA Translation: CAA24246.1 |
PIRi | A92444, ADRBA |
RefSeqi | NP_001075707.1, NM_001082238.1 XP_008256151.1, XM_008257929.2 XP_008256152.1, XM_008257930.2 XP_017197924.1, XM_017342435.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ADO | X-ray | 1.90 | A/B/C/D | 2-364 | [»] | |
1EWD | X-ray | 2.46 | A/B/C/D | 2-364 | [»] | |
1EWE | X-ray | 2.60 | A/B/C/D | 2-364 | [»] | |
1EX5 | X-ray | 2.20 | A/B/C/D | 2-364 | [»] | |
1J4E | X-ray | 2.65 | A/B/C/D | 2-364 | [»] | |
1ZAH | X-ray | 1.80 | A/B/C/D | 2-364 | [»] | |
1ZAI | X-ray | 1.76 | A/B/C/D | 2-364 | [»] | |
1ZAJ | X-ray | 1.89 | A/B/C/D | 2-364 | [»] | |
1ZAL | X-ray | 1.89 | A/B/C/D | 2-364 | [»] | |
2OT0 | X-ray | 2.05 | A/B/C/D | 2-364 | [»] | |
2OT1 | X-ray | 2.05 | A/B/C/D | 2-364 | [»] | |
2QUT | X-ray | 1.88 | A/B/C/D | 2-364 | [»] | |
2QUU | X-ray | 1.98 | A/B/C/D | 2-364 | [»] | |
2QUV | X-ray | 2.22 | A/B/C/D | 2-364 | [»] | |
3B8D | X-ray | 2.00 | A/B/C/D | 2-364 | [»] | |
3BV4 | X-ray | 1.70 | A | 5-344 | [»] | |
3DFN | X-ray | 1.86 | A/B/C/D | 2-364 | [»] | |
3DFO | X-ray | 1.94 | A/B/C/D | 2-364 | [»] | |
3DFP | X-ray | 2.05 | A/B/C/D | 2-364 | [»] | |
3DFQ | X-ray | 1.82 | A/B/C/D | 2-364 | [»] | |
3DFS | X-ray | 2.03 | A/B/C/D | 2-364 | [»] | |
3DFT | X-ray | 1.94 | A/B/C/D | 2-364 | [»] | |
3LGE | X-ray | 2.20 | A/B/C/D | 2-364 | [»] | |
3TU9 | X-ray | 2.09 | A/B/C/D | 2-364 | [»] | |
5F4X | X-ray | 1.84 | A/B/C/D | 2-364 | [»] | |
5TLE | X-ray | 1.58 | A/B/C/D | 2-364 | [»] | |
5TLH | X-ray | 2.20 | A/B/C/D | 2-364 | [»] | |
5TLW | X-ray | 2.29 | A/B/C/D | 2-364 | [»] | |
5TLZ | X-ray | 1.97 | A/B/C/D | 2-364 | [»] | |
5VY5 | electron microscopy | 2.60 | A/B/C/D | 2-364 | [»] | |
6ALD | X-ray | 2.30 | A/B/C/D | 2-364 | [»] | |
6MWQ | electron microscopy | 3.00 | A/B/C/D | 12-348 | [»] | |
6V20 | electron microscopy | 2.13 | A/B/C/D | 3-345 | [»] | |
PCDDBi | P00883 | |||||
SASBDBi | P00883 | |||||
SMRi | P00883 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 1172078, 2 interactors |
IntActi | P00883, 1 interactor |
MINTi | P00883 |
STRINGi | 9986.ENSOCUP00000008499 |
Chemistry databases
BindingDBi | P00883 |
ChEMBLi | CHEMBL4695 |
Protein family/group databases
MoonProti | P00883 |
PTM databases
iPTMneti | P00883 |
MetOSitei | P00883 |
Proteomic databases
PRIDEi | P00883 |
Genome annotation databases
Ensembli | ENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329 |
GeneIDi | 100009055 |
KEGGi | ocu:100009055 |
Organism-specific databases
CTDi | 226 |
Phylogenomic databases
eggNOGi | KOG1557, Eukaryota |
GeneTreei | ENSGT00950000182987 |
HOGENOMi | CLU_031243_1_0_1 |
InParanoidi | P00883 |
OMAi | DYREMLF |
OrthoDBi | 799973at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00109;UER00183 |
BRENDAi | 4.1.2.13, 1749 |
SABIO-RKi | P00883 |
Miscellaneous databases
EvolutionaryTracei | P00883 |
PROi | PR:P00883 |
Gene expression databases
Bgeei | ENSOCUG00000006329, Expressed in smooth muscle tissue and 17 other tissues |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
InterProi | View protein in InterPro IPR029768, Aldolase_I_AS IPR013785, Aldolase_TIM IPR000741, FBA_I |
Pfami | View protein in Pfam PF00274, Glycolytic, 1 hit |
PROSITEi | View protein in PROSITE PS00158, ALDOLASE_CLASS_I, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ALDOA_RABIT | |
Accessioni | P00883Primary (citable) accession number: P00883 Secondary accession number(s): Q28671 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 175 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families