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P07752 (ALF_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 96. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase, glycosomal

EC=4.1.2.13
Gene names
Name:ALD
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Subcellular location

Glycosome.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentGlycosome
Peroxisome
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentglycosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 372371Fructose-bisphosphate aldolase, glycosomal
PRO_0000216935

Sites

Active site1981Proton acceptor By similarity
Active site2401Schiff-base intermediate with dihydroxyacetone-P
Binding site661Substrate
Binding site1571Substrate
Site3721Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Experimental info

Sequence conflict254 – 2552GH → AT in AAA30153. Ref.3

Secondary structure

......................................................... 372
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07752 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 30F1F26F0D54211D

FASTA37241,178
        10         20         30         40         50         60 
MSKRVEVLLT QLPAYNRLKT PYEAELIETA KKMTAPGKGL LAADESTGSC SKRFAGIGLS 

        70         80         90        100        110        120 
NTAEHRRQYR ALMLECEGFE QYISGVILHD ETVYQKAKTG ETFPQYLRRR GVVPGIKTDC 

       130        140        150        160        170        180 
GLEPLVEGAK GEQMTAGLDG YIKRAKKYYA MGCRFCKWRN VYKIQNGTVS EAVVRFNAET 

       190        200        210        220        230        240 
LARYAILSQL CGLVPIVEPE VMIDGTHDIE TCQRVSQHVW SEVVSALHRH GVVWEGCLLK 

       250        260        270        280        290        300 
PNMVVPGAES GLKGHAEQVA EYTVKTLARV IPPALPGVTF LSGGLSEVMA SEYLNAMNNC 

       310        320        330        340        350        360 
PLPRPWKLTF SYARALQSSA IKRWGGKESG VEAGRRAFMH RAKMNSLAQL GKYNRADDDK 

       370 
DSQSLYVAGN TY 

« Hide

References

[1]"Structure and regulated expression of genes encoding fructose biphosphate aldolase in Trypanosoma brucei."
Clayton C.E.
EMBO J. 4:2997-3003(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genes encoding fructose bisphosphate aldolase in Trypanosoma brucei are interspersed with unrelated genes."
Vijayasarathy S., Ernest I., Itzhaki J., Sherman D., Mowatt M.R., Michels P.A.M., Clayton C.E.
Nucleic Acids Res. 18:2967-2975(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 427.
[3]"Characterization of the genes for fructose-bisphosphate aldolase in Trypanosoma brucei."
Marchand M., Poliszczak A., Gibson W.C., Wierenga R.K., Opperdoes F.R., Michels P.A.M.
Mol. Biochem. Parasitol. 29:65-76(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases."
Chudzik D.M., Michels P.A.M., de Walque S., Hol W.G.J.
J. Mol. Biol. 300:697-707(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-371.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03061 mRNA. Translation: CAA26867.1.
X52586 Genomic DNA. Translation: CAA36819.1.
M19994 Genomic DNA. Translation: AAA30153.1.
PIRADUT. A24678.
A54500.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F2JX-ray1.90A2-371[»]
ProteinModelPortalP07752.
SMRP07752. Positions 2-358.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP07752.
ChEMBLCHEMBL4916.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP07752.
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

EvolutionaryTraceP07752.

Entry information

Entry nameALF_TRYBB
AccessionPrimary (citable) accession number: P07752
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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