Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9U5N6 (Q9U5N6_LEIME) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase RuleBase RU003994
EC=4.1.2.13 RuleBase RU003994
Gene names
Name:ald EMBL CAB55315.1
OrganismLeishmania mexicana EMBL CAB55315.1
Taxonomic identifier5665 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmaniinae › Leishmania ›

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. RuleBase RU003994

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. RuleBase RU004257

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family. RuleBase RU003994

Ontologies

Keywords
   Biological processGlycolysis RuleBase RU003994
   Molecular functionLyase RuleBase RU003994 EMBL CAB55315.1
   Technical term3D-structure PDB 2QDH PDB 2QAP PDB 1EPX PDB 2QDG
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q9U5N6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 4EE4D9CDFA9126DB

FASTA37140,837
        10         20         30         40         50         60 
MSRVTVLQSQ LPAYNRLKTP YESELIATVK KLTTPGKGLL AADESIGSCT KRFQPIGLSN 

        70         80         90        100        110        120 
TEEHRRQYRA LMLEAEGFEQ YISGVILHDE TVGQKASNGQ TFPEYLTARG VVPGIKTDMG 

       130        140        150        160        170        180 
LCPLLEGAEG EQMTEGLDGY VKRASAYYKK GCRFCKWRNV YKIQNGTVSE SAVRFNAETL 

       190        200        210        220        230        240 
ARYAILSQMS GLVPIVEPEV MIDGKHDIDT CQRVSEHVWR EVVAALQRHG VIWEGCLLKP 

       250        260        270        280        290        300 
NMVVPGAESG KTAAPEQVAH YTVMTLARTM PAMLPGVMFL SGGLSEVQAS EYLNAINNSP 

       310        320        330        340        350        360 
LPRPYFLSFS YARALQSSAL KAWGGKESGL AAGRRAFLHR ARMNSMAQLG KYKRSDDDAS 

       370 
SSSLYVKGNT Y

« Hide

References

[1]"Cloning and characterization of Leishmania mexicana fructose-1,6-bisphosphate aldolase."
de Walque S., Opperdoes F.R., Michels P.A.
Mol. Biochem. Parasitol. 103:279-283(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: NHOM/BZ/84/BEL46 EMBL CAB55315.1.
[2]"Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases."
Chudzik D.M., Michels P.A., de Walque S., Hol W.G.
J. Mol. Biol. 300:697-707(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-370.
[3]"Carboxy-terminus recruitment induced by substrate binding in eukaryotic fructose bis-phosphate aldolases."
Lafrance-Vanasse J., Sygusch J.
Biochemistry 46:9533-9540(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ243322 Genomic DNA. Translation: CAB55315.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EPXX-ray1.80A/B/C/D1-370[»]
2QAPX-ray1.59A/B/C/D1-371[»]
2QDGX-ray2.20A/B/C/D1-371[»]
2QDHX-ray1.90A/B/C/D1-371[»]
ProteinModelPortalQ9U5N6.
SMRQ9U5N6. Positions 1-366.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA4.1.2.13. 1480.
SABIO-RKQ9U5N6.
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

ChEMBLCHEMBL4509.
EvolutionaryTraceQ9U5N6.

Entry information

Entry nameQ9U5N6_LEIME
AccessionPrimary (citable) accession number: Q9U5N6
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info