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Q8SSM8 (ALF_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. 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

EC=4.1.2.13
Gene names
Ordered Locus Names:ECU01_0240
OrganismEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]
Taxonomic identifier284813 [NCBI]
Taxonomic lineageEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
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.

Developmental stage

Expressed in late sporogonial stages.

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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

Chain1 – 338338Fructose-bisphosphate aldolase
PRO_0000381751

Sites

Active site1791Proton acceptor By similarity
Active site2211Schiff-base intermediate with dihydroxyacetone-P By similarity
Binding site501Substrate By similarity
Binding site1381Substrate By similarity

Secondary structure

....................................................... 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8SSM8 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 2158A1DAE05A7AF9

FASTA33837,917
        10         20         30         40         50         60 
MMDCDHLLRL GMTAKKILEN GKGILAADET PKTLGRRFEK LGITNTEENR RKFREILFST 

        70         80         90        100        110        120 
KGIERYIGGV ILNQETFEQT SGSGVPLTEL LKKKGIEIGI KLDKGLIDYK EKEKISVGLE 

       130        140        150        160        170        180 
DLDLRCKSSA FKDATFAKWR SLFYFYDGIP SEDCINENCS ILAKYAIICQ KNGLVPIVEP 

       190        200        210        220        230        240 
EVFLEGDYSM KRSYEVTRQI LSTLMKYLNY ELVYIPGVLI KASYVTSGQL SNEKYTPKKV 

       250        260        270        280        290        300 
ATFTLRALLS TIPCGIPGIV FLSGGHGSED AIGFLNAINM ERGCRTWSLS FSFARALTDG 

       310        320        330 
VLETWRGDDS NIEEAQKILL ETSFKACRGA EGKLWDQE 

« Hide

References

[1]"Sequence and analysis of chromosome I of the amitochondriate intracellular parasite Encephalitozoon cuniculi (Microspora)."
Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M., Weissenbach J., Saurin W., Vivares C.P.
Genome Res. 11:198-207(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.
[2]"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi."
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.
Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-M1.
[3]"Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi (microsporidia): a reference map for proteins expressed in late sporogonial stages."
Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.
Proteomics 6:3625-3635(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL391737 Genomic DNA. Translation: CAD24894.1.
RefSeqXP_965859.1. XM_960766.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MBDX-ray2.00A1-338[»]
3MBFX-ray2.37A1-338[»]
3QRHX-ray2.00A1-338[»]
ProteinModelPortalQ8SSM8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6035.ECU01_0240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID860198.
KEGGecu:ECU01_0240.

Organism-specific databases

EuPathDBMicrosporidiaDB:ECU01_0240.

Phylogenomic databases

eggNOGCOG3588.
HOGENOMHOG000220876.
KOK01623.
OMADMEHCQY.
OrthoDBEOG7M0P2G.

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]
ProtoNetSearch...

Other

EvolutionaryTraceQ8SSM8.

Entry information

Entry nameALF_ENCCU
AccessionPrimary (citable) accession number: Q8SSM8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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