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Q5NVR5 (ALDOA_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer. Interacts with SNX9 and WAS By similarity.

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.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from sequence or structural similarity. Source: UniProtKB

protein homotetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 364363Fructose-bisphosphate aldolase A
PRO_0000230295

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P
Binding site561Substrate
Binding site1471Substrate
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

Sequences

Sequence LengthMass (Da)Tools
Q5NVR5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4DAED62BFE37CD33

FASTA36439,448
        10         20         30         40         50         60 
MPYQYPALTP 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 
TQKFSHEEIV MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF 

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


NHAY 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR925940 mRNA. Translation: CAI29598.1.
RefSeqNP_001127068.1. NM_001133596.2.

3D structure databases

ProteinModelPortalQ5NVR5.
SMRQ5NVR5. Positions 2-364.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5NVR5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174098.
KEGGpon:100174098.

Organism-specific databases

CTD226.

Phylogenomic databases

HOVERGENHBG002386.
InParanoidQ5NVR5.
KOK01623.

Enzyme and pathway databases

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...

Entry information

Entry nameALDOA_PONAB
AccessionPrimary (citable) accession number: Q5NVR5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 60 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways