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P07752

- ALF_TRYBB

UniProt

P07752 - ALF_TRYBB

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Protein
Fructose-bisphosphate aldolase, glycosomal
Gene
ALD
Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661Substrate
Binding sitei157 – 1571Substrate
Active sitei198 – 1981Proton acceptor By similarity
Active sitei240 – 2401Schiff-base intermediate with dihydroxyacetone-P
Sitei372 – 3721Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

SABIO-RKiP07752.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase, glycosomal (EC:4.1.2.13)
Gene namesi
Name:ALD
OrganismiTrypanosoma brucei brucei
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Subcellular locationi

GO - Cellular componenti

  1. glycosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Glycosome, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 372371Fructose-bisphosphate aldolase, glycosomal
PRO_0000216935Add
BLAST

Interactioni

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113
Helixi13 – 153
Helixi23 – 3311
Beta strandi39 – 435
Helixi47 – 559
Turni56 – 583
Helixi63 – 7412
Helixi79 – 813
Beta strandi83 – 886
Helixi90 – 945
Beta strandi100 – 1023
Helixi103 – 1097
Beta strandi113 – 1175
Beta strandi122 – 1243
Beta strandi126 – 1294
Beta strandi133 – 1353
Helixi141 – 15010
Beta strandi155 – 1628
Helixi171 – 19020
Beta strandi194 – 2018
Helixi209 – 23022
Helixi234 – 2363
Helixi256 – 27015
Beta strandi277 – 2804
Helixi287 – 29711
Beta strandi306 – 3138
Helixi314 – 32411
Helixi328 – 3303
Helixi331 – 34919
Helixi355 – 3573

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F2JX-ray1.90A2-371[»]
ProteinModelPortaliP07752.
SMRiP07752. Positions 2-358.

Miscellaneous databases

EvolutionaryTraceiP07752.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07752-1 [UniParc]FASTAAdd to Basket

« Hide

MSKRVEVLLT QLPAYNRLKT PYEAELIETA KKMTAPGKGL LAADESTGSC    50
SKRFAGIGLS NTAEHRRQYR ALMLECEGFE QYISGVILHD ETVYQKAKTG 100
ETFPQYLRRR GVVPGIKTDC GLEPLVEGAK GEQMTAGLDG YIKRAKKYYA 150
MGCRFCKWRN VYKIQNGTVS EAVVRFNAET LARYAILSQL CGLVPIVEPE 200
VMIDGTHDIE TCQRVSQHVW SEVVSALHRH GVVWEGCLLK PNMVVPGAES 250
GLKGHAEQVA EYTVKTLARV IPPALPGVTF LSGGLSEVMA SEYLNAMNNC 300
PLPRPWKLTF SYARALQSSA IKRWGGKESG VEAGRRAFMH RAKMNSLAQL 350
GKYNRADDDK DSQSLYVAGN TY 372
Length:372
Mass (Da):41,178
Last modified:January 23, 2007 - v2
Checksum:i30F1F26F0D54211D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti254 – 2552GH → AT in AAA30153. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03061 mRNA. Translation: CAA26867.1.
X52586 Genomic DNA. Translation: CAA36819.1.
M19994 Genomic DNA. Translation: AAA30153.1.
PIRiA24678. ADUT.
A54500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03061 mRNA. Translation: CAA26867.1 .
X52586 Genomic DNA. Translation: CAA36819.1 .
M19994 Genomic DNA. Translation: AAA30153.1 .
PIRi A24678. ADUT.
A54500.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F2J X-ray 1.90 A 2-371 [» ]
ProteinModelPortali P07752.
SMRi P07752. Positions 2-358.
ModBasei Search...

Chemistry

BindingDBi P07752.
ChEMBLi CHEMBL4916.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
SABIO-RKi P07752.

Miscellaneous databases

EvolutionaryTracei P07752.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view ]
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiALF_TRYBB
AccessioniPrimary (citable) accession number: P07752
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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