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Q9GP32

- ALF_ECHMU

UniProt

Q9GP32 - ALF_ECHMU

Protein

Fructose-bisphosphate aldolase

Gene

FBPA

Organism
Echinococcus multilocularis (Fox tapeworm)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 sitei56 – 561SubstrateBy similarity
    Binding sitei147 – 1471SubstrateBy similarity
    Active sitei188 – 1881Proton acceptorBy similarity
    Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-PBy similarity
    Sitei363 – 3631Necessary 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

    UniPathwayiUPA00109; UER00183.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase (EC:4.1.2.13)
    Gene namesi
    Name:FBPA
    OrganismiEchinococcus multilocularis (Fox tapeworm)
    Taxonomic identifieri6211 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesCestodaEucestodaCyclophyllideaTaeniidaeEchinococcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 363363Fructose-bisphosphate aldolasePRO_0000216933Add
    BLAST

    Proteomic databases

    PRIDEiQ9GP32.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9GP32.
    SMRiQ9GP32. Positions 2-363.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    Q9GP32-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRFVPYLCA EKMKELRENA SAIVAPGKGL LAADESTNTI GKRFAAINLE    50
    NTEENRRAYR ELLFTTDPEF AKHISGVILF HETVYQKTKD GKPFVELLRE 100
    RGVLPGIKVD LGVVPLGGTA DECTTQGLDN LAQRCAQYYN DGCRFAKWRC 150
    VLKISSHNPS YLAMLENANV LARYAFICQQ NGLVPIVEPE VLPDGDHDLE 200
    TAQRVTEQVL SFVYKALADH HVYLEGTLLK PNMVTCGQSC TKKYSVEDNA 250
    RATVEALQRT VPVAVPGVVF LSGGQSELDA TRNLNAINKY PGKKPWALSF 300
    SFGRALQASA IAAWQGKPEN VKAGQAEFLQ LAKANGAASL GKFEGELKTA 350
    AGQKSLFVAN HAY 363
    Length:363
    Mass (Da):39,727
    Last modified:March 1, 2001 - v1
    Checksum:i37862DEC55BA2B70
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ292376 mRNA. Translation: CAC18550.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ292376 mRNA. Translation: CAC18550.1 .

    3D structure databases

    ProteinModelPortali Q9GP32.
    SMRi Q9GP32. Positions 2-363.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9GP32.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .

    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. "mRNA trans-splicing in the human parasitic cestode Echinococcus multilocularis."
      Brehm K., Jensen K., Frosch M.
      J. Biol. Chem. 275:38311-38318(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: H-95.

    Entry informationi

    Entry nameiALF_ECHMU
    AccessioniPrimary (citable) accession number: Q9GP32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3