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P07752

- ALF_TRYBB

UniProt

P07752 - ALF_TRYBB

Protein

Fructose-bisphosphate aldolase, glycosomal

Gene

ALD

Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 acceptorBy 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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    SABIO-RKP07752.
    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

    Keywords - Cellular componenti

    Glycosome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 372371Fructose-bisphosphate aldolase, glycosomalPRO_0000216935Add
    BLAST

    Interactioni

    Structurei

    Secondary structure

    1
    372
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti254 – 2552GH → AT in AAA30153. (PubMed:3386689)Curated

    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...
    MobiDBi Search...

    Chemistry

    BindingDBi P07752.
    ChEMBLi CHEMBL4916.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    SABIO-RK 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: October 1, 2014
    This is version 99 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