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Reviewed, UniProtKB/Swiss-Prot Q5R1X4 (ALDOC_PANTR)

Last modified January 19, 2010. Version 40. 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 C
    EC=4.1.2.13
Alternative name(s):
    Brain-type aldolase
Gene names
Name: ALDOC
Synonyms: ALDC
OrganismPan troglodytes (Chimpanzee)
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

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. Interacts with ATP6V1E1 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 processfructose 1,6-bisphosphate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 C
PRO_0000216950

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 residue391Phosphoserine By similarity
Modified residue1191Phosphothreonine By similarity
Modified residue1471N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R1X4-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5064305BB473D8AE

FASTA36439,527
        10         20         30         40         50         60 
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR 

        70         80         90        100        110        120 
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFIRTILD KGIVVGIKVD KGVVPLAGTD 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ 

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

       250        260        270        280        290        300 
PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LNAWRGQRDN AEAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA 


NHAY 

« Hide

References

[1]Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y., Osada N., Hashimoto K.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cerebellum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB188273 mRNA. Translation: BAD74024.1.
RefSeqNP_001009147.1.

3D structure databases

SMRQ5R1X4. Positions 3-344.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5R1X4.

Genome annotation databases

EnsemblENSPTRT00000016458; ENSPTRP00000015230; ENSPTRG00000008923; Pan troglodytes. [Genome view]
GeneID493951.
KEGGptr:493951.

Organism-specific databases

CTD493951.

Phylogenomic databases

eggNOGprNOG14846.
HOVERGENQ5R1X4.
InParanoidQ5R1X4.

Enzyme and pathway databases

BRENDA4.1.2.13. 264977.

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]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALDOC_PANTR
AccessionPrimary (citable) accession number: Q5R1X4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 40 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