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P54216

- ALF1_CAEEL

UniProt

P54216 - ALF1_CAEEL

Protein

Fructose-bisphosphate aldolase 1

Gene

aldo-1

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 sitei189 – 1891Proton acceptorBy similarity
    Active sitei231 – 2311Schiff-base intermediate with dihydroxyacetone-PBy similarity
    Sitei366 – 3661Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

    GO - Molecular functioni

    1. fructose-bisphosphate aldolase activity Source: UniProtKB
    2. identical protein binding Source: IntAct

    GO - Biological processi

    1. glycolytic process Source: UniProtKB

    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 1 (EC:4.1.2.13)
    Alternative name(s):
    Aldolase CE-1
    Short name:
    CE1
    Gene namesi
    Name:aldo-1
    ORF Names:T05D4.1
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome III

    Organism-specific databases

    WormBaseiT05D4.1; CE16341; WBGene00011474; aldo-1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: WormBase
    2. sarcomere Source: WormBase
    3. striated muscle dense body Source: WormBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 366366Fructose-bisphosphate aldolase 1PRO_0000216928Add
    BLAST

    Proteomic databases

    PaxDbiP54216.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Developmental stagei

    All stages of development.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-327260,EBI-327260

    Protein-protein interaction databases

    BioGridi41956. 1 interaction.
    DIPiDIP-25939N.
    IntActiP54216. 1 interaction.
    MINTiMINT-1094145.

    Structurei

    3D structure databases

    ProteinModelPortaliP54216.
    SMRiP54216. Positions 8-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3588.
    HOGENOMiHOG000220876.
    InParanoidiP54216.
    KOiK01623.
    PhylomeDBiP54216.

    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.

    P54216-1 [UniParc]FASTAAdd to Basket

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    MASYSQFLTK AQEDELRSIA NAIVTPGKGI LAADESTGSM DKRLNSIGLE    50
    NTEENRRKYR QLLFTAGADL NKYISGVIMF HETFYQKTDD GKPFTALLQE 100
    QGIIPGIKVD KGVVPMAGTI GEGTTQGLDD LNARCAQYKK DGAQFAKWRC 150
    VHKISSTTPS VTALKEIASN LGSRYASICQ QNGLVPIVEP EILPDGEHCL 200
    ARGQKITETV LSYVYHALNE HHVFLEGTLL KPNMVTSGQS FTGEKPSNAD 250
    IGLATVTALQ RGVPSAVPGV VFLSGGQSEE DATLNLNAIN QVSGKKPWAL 300
    TFSYGRALQA SCLAKWAGKD ENIAAAQEVL LHRAQVNSLA SVGKYTGDAS 350
    ADAAASQSLF VANHSY 366
    Length:366
    Mass (Da):39,240
    Last modified:October 1, 1996 - v1
    Checksum:i5B9F91D486FFAEB5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti172 – 1732GS → A in CAB03291. (PubMed:9851916)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83738 mRNA. Translation: BAA12091.1.
    Z81115 Genomic DNA. Translation: CAB03291.1.
    PIRiT24514.
    RefSeqiNP_741281.1. NM_171235.3.
    UniGeneiCel.6851.

    Genome annotation databases

    GeneIDi176788.
    KEGGicel:CELE_T05D4.1.
    UCSCiT05D4.1.1. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83738 mRNA. Translation: BAA12091.1 .
    Z81115 Genomic DNA. Translation: CAB03291.1 .
    PIRi T24514.
    RefSeqi NP_741281.1. NM_171235.3.
    UniGenei Cel.6851.

    3D structure databases

    ProteinModelPortali P54216.
    SMRi P54216. Positions 8-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 41956. 1 interaction.
    DIPi DIP-25939N.
    IntActi P54216. 1 interaction.
    MINTi MINT-1094145.

    Proteomic databases

    PaxDbi P54216.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 176788.
    KEGGi cel:CELE_T05D4.1.
    UCSCi T05D4.1.1. c. elegans.

    Organism-specific databases

    CTDi 176788.
    WormBasei T05D4.1 ; CE16341 ; WBGene00011474 ; aldo-1.

    Phylogenomic databases

    eggNOGi COG3588.
    HOGENOMi HOG000220876.
    InParanoidi P54216.
    KOi K01623.
    PhylomeDBi P54216.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .

    Miscellaneous databases

    NextBioi 894008.

    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. "Caenorhabditis elegans has two isozymic forms, CE-1 and CE-2, of fructose-1,6-bisphosphate aldolase which are encoded by different genes."
      Inoue T., Yatsuki H., Kusakabe T., Joh K., Hori K.
      Arch. Biochem. Biophys. 339:226-234(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Bristol N2.
    2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.

    Entry informationi

    Entry nameiALF1_CAEEL
    AccessioniPrimary (citable) accession number: P54216
    Secondary accession number(s): O45747
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3