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P00883 (ALDOA_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase A

EC=4.1.2.13
Alternative name(s):
Muscle-type aldolase
Gene names
Name:ALDOA
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein. Ref.14

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Ref.16

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Tetramer. Interacts with SNX9 and WAS. Ref.15 Ref.16

Post-translational modification

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

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.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3 Ref.4
Chain2 – 364363Fructose-bisphosphate aldolase A
PRO_0000216938

Sites

Active site1881Proton acceptor Ref.8 Ref.9
Active site2301Schiff-base intermediate with dihydroxyacetone-P Ref.8 Ref.9
Binding site431Substrate
Binding site3041Substrate
Site731Essential for substrate cleavage
Site1081Essential for substrate cleavage
Site1471Alkylation inactivates the enzyme
Site3621Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base
Site3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue361Phosphoserine By similarity
Modified residue391Phosphoserine By similarity
Modified residue421N6-acetyllysine By similarity
Modified residue461Phosphoserine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue1111N6-malonyllysine By similarity
Modified residue3121N6-malonyllysine By similarity
Modified residue3301N6-acetyllysine By similarity
Modified residue3611Deamidated asparagine; in form beta

Experimental info

Mutagenesis351E → A: Reduces activity 14-fold. Ref.12
Mutagenesis431R → A: Reduces activity 14-fold. Ref.12
Mutagenesis1291D → V: Alters protein-protein interactions, leading to a dimeric protein.
Mutagenesis1471K → A: Loss of activity. Ref.12
Mutagenesis1881E → A: Reduces activity over 100-fold. Ref.13
Mutagenesis1881E → Q: Reduces activity over 1000-fold. Ref.13
Mutagenesis1901E → Q: Reduces activity 20-fold. Ref.13
Mutagenesis2301K → M: Loss of activity. Ref.13
Mutagenesis3041R → A: Reduces activity 400-fold. Ref.12
Sequence conflict351E → Q AA sequence Ref.4
Sequence conflict274 – 2763GQS → SQE AA sequence Ref.6
Sequence conflict2761S → E AA sequence Ref.6
Sequence conflict294 – 2963KPW → WPK AA sequence Ref.6
Sequence conflict3541S → R in CAA24246. Ref.7

Secondary structure

................................................................ 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00883 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E61BCBC60F668324

FASTA36439,343
        10         20         30         40         50         60 
MPHSHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR 

        70         80         90        100        110        120 
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC 

       250        260        270        280        290        300 
TQKYSHEEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFIS 


NHAY 

« Hide

References

[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]"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).
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02300 mRNA. Translation: AAA31156.1.
V00876 mRNA. Translation: CAA24245.1.
V00877 mRNA. Translation: CAA24246.1.
PIRADRBA. A92444.
RefSeqNP_001075707.1. NM_001082238.1.
UniGeneOcu.864.

3D structure databases

PDBe
RCSB PDB
PDBj
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/D2-363[»]
1ZAHX-ray1.80A/B/C/D2-363[»]
1ZAIX-ray1.76A/B/C/D2-363[»]
1ZAJX-ray1.89A/B/C/D2-363[»]
1ZALX-ray1.89A/B/C/D2-363[»]
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[»]
ProteinModelPortalP00883.
SMRP00883. Positions 2-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00883. 1 interaction.
MINTMINT-7995296.
STRING9986.ENSOCUP00000020204.

Chemistry

BindingDBP00883.
ChEMBLCHEMBL4695.

Proteomic databases

PRIDEP00883.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329.
GeneID100009055.

Organism-specific databases

CTD226.

Phylogenomic databases

eggNOGCOG3588.
GeneTreeENSGT00390000010235.
HOGENOMHOG000220876.
HOVERGENHBG002386.

Enzyme and pathway databases

SABIO-RKP00883.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00883.

Entry information

Entry nameALDOA_RABIT
AccessionPrimary (citable) accession number: P00883
Secondary accession number(s): Q28671
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways