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Reviewed, UniProtKB/Swiss-Prot Q5NVR5 (ALDOA_PONAB)

Last modified November 3, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
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)

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 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
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

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 residue31Phosphotyrosine By similarity
Modified residue51Phosphotyrosine By similarity
Modified residue131N6-acetyllysine By similarity
Modified residue361Phosphoserine By similarity
Modified residue391Phosphoserine By similarity
Modified residue421N6-acetyllysine By similarity
Modified residue461Phosphoserine By similarity
Modified residue651Phosphothreonine By similarity
Modified residue1081N6-acetyllysine By similarity
Modified residue2041Phosphotyrosine By similarity
Modified residue2231Phosphotyrosine By similarity
Modified residue2351Phosphothreonine By similarity
Modified residue2411Phosphothreonine By similarity
Modified residue3301N6-acetyllysine By similarity
Modified residue3541Phosphoserine By similarity
Modified residue3561Phosphoserine By similarity
Modified residue3641Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NVR5-1 [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

CR925940 mRNA. Translation: CAI29598.1.
RefSeqNP_001127068.1.
UniGenePab.18439

3D structure databases

SMRQ5NVR5. Positions 1-363, 2-364.
ModBaseSearch...

Genome annotation databases

GeneID100174098.

Organism-specific databases

CTD100174098.

Phylogenomic databases

HOVERGENQ5NVR5.

Enzyme and pathway databases

BRENDA4.1.2.13. 269192.

Family and domain databases

InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11627. Aldolase_I. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
ProDomPD001128. Aldolase_I. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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 3, 2009
This is version 38 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents