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P00883

- ALDOA_RABIT

UniProt

P00883 - ALDOA_RABIT

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Protein
Fructose-bisphosphate aldolase A
Gene
ALDOA
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.1 Publication

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431Substrate
Sitei73 – 731Essential for substrate cleavage
Sitei108 – 1081Essential for substrate cleavage
Sitei147 – 1471Alkylation inactivates the enzyme
Active sitei188 – 1881Proton acceptor2 Publications
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P2 Publications
Binding sitei304 – 3041Substrate
Sitei362 – 3621Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base
Sitei364 – 3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. fructose binding Source: Ensembl
  2. fructose-bisphosphate aldolase activity Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. ATP biosynthetic process Source: Ensembl
  2. fructose 1,6-bisphosphate metabolic process Source: Ensembl
  3. fructose metabolic process Source: Ensembl
  4. glycolytic process Source: UniProtKB
  5. muscle cell cellular homeostasis Source: Ensembl
  6. protein homotetramerization Source: UniProtKB
  7. regulation of cell shape Source: Ensembl
  8. striated muscle contraction Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

SABIO-RKP00883.
UniPathwayiUPA00109; UER00183.

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Chromosome 6

Subcellular locationi

CytoplasmmyofibrilsarcomereI band. CytoplasmmyofibrilsarcomereM 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 Ca2+.1 Publication

GO - Cellular componenti

  1. I band Source: UniProtKB-SubCell
  2. M band Source: UniProtKB-SubCell
  3. actin cytoskeleton Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351E → A: Reduces activity 14-fold. 1 Publication
Mutagenesisi43 – 431R → A: Reduces activity 14-fold. 1 Publication
Mutagenesisi129 – 1291D → V: Alters protein-protein interactions, leading to a dimeric protein.
Mutagenesisi147 – 1471K → A: Loss of activity. 1 Publication
Mutagenesisi188 – 1881E → A: Reduces activity over 100-fold. 1 Publication
Mutagenesisi188 – 1881E → Q: Reduces activity over 1000-fold. 1 Publication
Mutagenesisi190 – 1901E → Q: Reduces activity 20-fold. 1 Publication
Mutagenesisi230 – 2301K → M: Loss of activity. 1 Publication
Mutagenesisi304 – 3041R → A: Reduces activity 400-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 364363Fructose-bisphosphate aldolase A
PRO_0000216938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361Phosphoserine By similarity
Modified residuei39 – 391Phosphoserine By similarity
Modified residuei42 – 421N6-acetyllysine By similarity
Modified residuei46 – 461Phosphoserine By similarity
Modified residuei108 – 1081N6-acetyllysine By similarity
Modified residuei111 – 1111N6-malonyllysine By similarity
Modified residuei312 – 3121N6-malonyllysine By similarity
Modified residuei330 – 3301N6-acetyllysine By similarity
Modified residuei361 – 3611Deamidated asparagine; in form beta

Post-translational modificationi

Asn-361 in form alpha is deaminated to Asp in form beta.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP00883.

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+.4 Publications

Protein-protein interaction databases

IntActiP00883. 1 interaction.
MINTiMINT-7995296.
STRINGi9986.ENSOCUP00000020204.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314
Beta strandi29 – 335
Helixi37 – 459
Turni46 – 483
Helixi53 – 6412
Helixi68 – 703
Turni71 – 733
Beta strandi74 – 796
Helixi81 – 844
Turni89 – 913
Helixi94 – 996
Turni100 – 1023
Beta strandi104 – 1085
Beta strandi113 – 1153
Beta strandi119 – 1213
Beta strandi123 – 1253
Helixi131 – 14010
Beta strandi145 – 1528
Beta strandi155 – 1573
Helixi161 – 18020
Beta strandi184 – 1918
Helixi199 – 21921
Helixi224 – 2263
Helixi246 – 25813
Beta strandi267 – 2704
Helixi277 – 28913
Beta strandi290 – 2923
Beta strandi296 – 3038
Helixi304 – 31411
Helixi318 – 3203
Helixi321 – 33818
Turni339 – 3413
Beta strandi345 – 3473
Beta strandi349 – 3524
Beta strandi358 – 3603
Helixi361 – 3633

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ADOX-ray1.90A/B/C/D2-364[»]
1EWDX-ray2.46A/B/C/D2-364[»]
1EWEX-ray2.60A/B/C/D2-364[»]
1EX5X-ray2.20A/B/C/D2-364[»]
1J4EX-ray2.65A/B/C/D2-364[»]
1ZAHX-ray1.80A/B/C/D2-364[»]
1ZAIX-ray1.76A/B/C/D2-364[»]
1ZAJX-ray1.89A/B/C/D2-364[»]
1ZALX-ray1.89A/B/C/D2-364[»]
2OT0X-ray2.05A/B/C/D2-364[»]
2OT1X-ray2.05A/B/C/D2-364[»]
2QUTX-ray1.88A/B/C/D2-364[»]
2QUUX-ray1.98A/B/C/D2-364[»]
2QUVX-ray2.22A/B/C/D2-364[»]
3B8DX-ray2.00A/B/C/D2-364[»]
3BV4X-ray1.70A5-344[»]
3DFNX-ray1.86A/B/C/D2-364[»]
3DFOX-ray1.94A/B/C/D2-364[»]
3DFPX-ray2.05A/B/C/D2-364[»]
3DFQX-ray1.82A/B/C/D2-364[»]
3DFSX-ray2.03A/B/C/D2-364[»]
3DFTX-ray1.94A/B/C/D2-364[»]
3LGEX-ray2.20A/B/C/D2-364[»]
3TU9X-ray2.09A/B/C/D2-364[»]
6ALDX-ray2.30A/B/C/D2-364[»]
ProteinModelPortaliP00883.
SMRiP00883. Positions 2-364.

Miscellaneous databases

EvolutionaryTraceiP00883.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00883-1 [UniParc]FASTAAdd to Basket

« Hide

MPHSHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE    50
NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS 100
KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC 150
VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK 200
RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKYSHEEIA 250
MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF 300
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG 350
AAASESLFIS NHAY 364
Length:364
Mass (Da):39,343
Last modified:January 23, 2007 - v2
Checksum:iE61BCBC60F668324
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351E → Q AA sequence 1 Publication
Sequence conflicti274 – 2763GQS → SQE AA sequence 1 Publication
Sequence conflicti276 – 2761S → E AA sequence 1 Publication
Sequence conflicti294 – 2963KPW → WPK AA sequence 1 Publication
Sequence conflicti354 – 3541S → R in CAA24246. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02300 mRNA. Translation: AAA31156.1.
V00876 mRNA. Translation: CAA24245.1.
V00877 mRNA. Translation: CAA24246.1.
PIRiA92444. ADRBA.
RefSeqiNP_001075707.1. NM_001082238.1.
UniGeneiOcu.864.

Genome annotation databases

EnsembliENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329.
GeneIDi100009055.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UniGenei Ocu.864.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
6ALD X-ray 2.30 A/B/C/D 2-364 [» ]
ProteinModelPortali P00883.
SMRi P00883. Positions 2-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00883. 1 interaction.
MINTi MINT-7995296.
STRINGi 9986.ENSOCUP00000020204.

Chemistry

BindingDBi P00883.
ChEMBLi CHEMBL4695.

Proteomic databases

PRIDEi P00883.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSOCUT00000009869 ; ENSOCUP00000008499 ; ENSOCUG00000006329 .
GeneIDi 100009055.

Organism-specific databases

CTDi 226.

Phylogenomic databases

eggNOGi COG3588.
GeneTreei ENSGT00390000010235.
HOGENOMi HOG000220876.
HOVERGENi HBG002386.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
SABIO-RK P00883.

Miscellaneous databases

EvolutionaryTracei P00883.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view ]
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The complete nucleotide sequence for rabbit muscle aldolase A messenger RNA."
    Tolan D.R., Amsden A.B., Putney S.D., Urdea M.S., Penhoet E.E.
    J. Biol. Chem. 259:1127-1131(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The amino acid sequence of rabbit muscle aldolase."
    Sajgo M., Hajos G.
    Acta Biochim. Biophys. Acad. Sci. Hung. 9:239-241(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-364.
    Tissue: Muscle.
  3. "Amino acid sequence of rabbit muscle aldolase and the structure of the active center."
    Lai C.-Y., Nakai N., Chang D.
    Science 183:1204-1206(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-364.
    Tissue: Muscle.
  4. "Studies on the structure of rabbit muscle aldolase. Ordering of the tryptic peptides; sequence of 164 amino acid residues in the NH2-terminal BrCN peptide."
    Nakai N., Chang D., Lai C.-Y.
    Arch. Biochem. Biophys. 166:347-357(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-165.
  5. "Extended amino acid sequences around the active-site lysine residue of class-I fructose 1,6-bisphosphate aldolases from rabbit muscle, sturgeon muscle, trout muscle and ox liver."
    Benfield P.A., Forcina B.G., Gibbons I., Perham R.N.
    Biochem. J. 183:429-444(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 174-201, SEQUENCE REVISION.
  6. "Studies on the structure of rabbit muscle aldolase. Determination of the primary structure of the COOH-terminal BrCN peptide; the complete sequence of the subunit polypeptide chain."
    Lai C.-Y.
    Arch. Biochem. Biophys. 166:358-368(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 252-364, SEQUENCE REVISION.
  7. "A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
    Putney S.D., Herlihy W.C., Schimmel P.R.
    Nature 302:718-721(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-56 AND 350-364.
  8. "Identification of the histidyl residue of rabbit muscle aldolase alkylated by N-bromoacetylethanolamine phosphate."
    Hartman F.C., Welch M.H.
    Biochem. Biophys. Res. Commun. 57:85-92(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  9. "Affinity labeling of a previously undetected essential lysyl residue in class I fructose bisphosphate aldolase."
    Hartman F.C., Brown J.P.
    J. Biol. Chem. 251:3057-3062(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  10. "Identification of the C-1-phosphate-binding arginine residue of rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled peptide by chemisorption chromatography."
    Patthy L., Varadi A., Thesz J., Kovacs K.
    Eur. J. Biochem. 99:309-313(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE-BINDING SITE.
  11. "The effect of calcium ions on subcellular localization of aldolase-FBPase complex in skeletal muscle."
    Mamczur P., Rakus D., Gizak A., Dus D., Dzugaj A.
    FEBS Lett. 579:1607-1612(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBP2, SUBCELLULAR LOCATION.
  12. "Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase."
    Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.
    Proteins 72:209-216(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBP2.
  13. "Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase."
    Blom N., Sygusch J.
    Nat. Struct. Biol. 4:36-39(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  14. "Structure of a fructose-1,6-bis(phosphate) aldolase liganded to its natural substrate in a cleavage-defective mutant at 2.3 A."
    Choi K.H., Mazurkie A.S., Morris A.J., Utheza D., Tolan D.R., Allen K.N.
    Biochemistry 38:12655-12664(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-345 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF GLU-35; ARG-43; LYS-147 AND ARG-304.
  15. "A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases."
    Maurady A., Zdanov A., de Moissac D., Beaudry D., Sygusch J.
    J. Biol. Chem. 277:9474-9483(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS), MUTAGENESIS OF GLU-188; GLU-190 AND LYS-230.
  16. "A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein."
    St-Jean M., Izard T., Sygusch J.
    J. Biol. Chem. 282:14309-14315(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH WAS, FUNCTION.
  17. "Structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant."
    Sherawat M., Tolan D.R., Allen K.N.
    Acta Crystallogr. D 64:543-550(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 5-344 OF MUTANT VAL-129, SUBUNIT.
  18. "Mechanism of aldolase control of sorting nexin 9 function in endocytosis."
    Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.
    J. Biol. Chem. 285:11983-11990(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SNX9, INTERACTION WITH SNX9, SUBUNIT, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiALDOA_RABIT
AccessioniPrimary (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: September 3, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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