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P53448 (ALDOC_CARAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. 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 C

EC=4.1.2.13
Alternative name(s):
Brain-type aldolase
Gene names
Name:aldoc
OrganismCarassius auratus (Goldfish)
Taxonomic identifier7957 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCarassius

Protein attributes

Sequence length363 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.

Tissue specificity

Expressed in brain but not in liver or muscle. Ref.1

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
Gene Ontology (GO)
   Biological_processfructose 1,6-bisphosphate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 363362Fructose-bisphosphate aldolase C
PRO_0000216953

Sites

Active site2301Schiff-base intermediate with dihydroxyacetone-P By similarity
Binding site561Substrate By similarity
Binding site1471Substrate By similarity
Site3631Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P53448 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 23ED53BABED42327

FASTA36339,475
        10         20         30         40         50         60 
MTHQYPALTT EQKRELQDIA QRIVAPGKGI LAADESTGSM AKRLNPIGVE NTEENRRLYR 

        70         80         90        100        110        120 
QLLFTADERM DKCIGGVIFF HETLYQKADD GTPFAKMIKD RGIVVGIKVD KGVVPLAGTN 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRS VLKISETSPS ELAIMENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AACYKALSDH HVYLEGTLLK PNMVTAGHSC 

       250        260        270        280        290        300 
PTKFSNQEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINNC PLTKPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LSAWRGVKEN EKAATEEFLK RAEANGLAAQ GKYVSSGMDG SAGQSLYVAN 


HAY 

« Hide

References

[1]"Identification of neuronal isozyme specific residues by comparison of goldfish aldolase C to other aldolases."
Berardini T.Z., Drygas-Williams M., Callard G.V., Tolan D.R.
Comp. Biochem. Physiol. 117A:471-476(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U36777 mRNA. Translation: AAA84887.1.

3D structure databases

ProteinModelPortalP53448.
SMRP53448. Positions 3-363.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP53448.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG002386.

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 nameALDOC_CARAU
AccessionPrimary (citable) accession number: P53448
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 65 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

PATHWAY comments

Index of metabolic and biosynthesis pathways