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P53449

- ALDOC_CHICK

UniProt

P53449 - ALDOC_CHICK

Protein

Fructose-bisphosphate aldolase C

Gene

ALDOC

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei3 – 31Schiff-base intermediate with dihydroxyacetone-P
    Sitei137 – 1371Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

    GO - Molecular functioni

    1. fructose-bisphosphate aldolase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. fructose 1,6-bisphosphate metabolic process Source: UniProtKB
    3. gluconeogenesis Source: Reactome
    4. glycolytic process Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    ReactomeiREACT_115534. Gluconeogenesis.
    REACT_115767. Glycolysis.
    UniPathwayiUPA00109; UER00183.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase C (EC:4.1.2.13)
    Alternative name(s):
    Brain-type aldolase
    Gene namesi
    Name:ALDOC
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 137›137Fructose-bisphosphate aldolase CPRO_0000216952Add
    BLAST

    Proteomic databases

    PRIDEiP53449.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP53449.
    SMRiP53449. Positions 1-117.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG002386.
    PhylomeDBiP53449.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Fragment.

    P53449-1 [UniParc]FASTAAdd to Basket

    « Hide

    LLKPNMVTPG HSCPTKYSPE EIAMATVTAL RRTVPPAVPG VTFLSGGQSE    50
    EEASINLNAI NTCPLVRPWA LTFSYGRALQ ASALSAWRGQ RDNANAATEE 100
    FVKRAEVNGL AALGKYEGSG DDSGAAGQSL YVANHAY 137
    Length:137
    Mass (Da):14,438
    Last modified:October 1, 1996 - v1
    Checksum:i2E70FB9213133D15
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25375 mRNA. Translation: AAA48589.1.
    S78291 mRNA. Translation: AAB34480.1.
    PIRiI51292.
    UniGeneiGga.4982.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25375 mRNA. Translation: AAA48589.1 .
    S78291 mRNA. Translation: AAB34480.1 .
    PIRi I51292.
    UniGenei Gga.4982.

    3D structure databases

    ProteinModelPortali P53449.
    SMRi P53449. Positions 1-117.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P53449.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG002386.
    PhylomeDBi P53449.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    Reactomei REACT_115534. Gluconeogenesis.
    REACT_115767. Glycolysis.

    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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Noncoordinate changes in the steady-state mRNA expressed from aldolase A and aldolase C genes during differentiation of chicken myoblasts."
      Meighan-Mantha R.L., Tolan D.R.
      J. Cell. Biochem. 57:423-431(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.

    Entry informationi

    Entry nameiALDOC_CHICK
    AccessioniPrimary (citable) accession number: P53449
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3