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Q9C2U0

- ALF_KLULA

UniProt

Q9C2U0 - ALF_KLULA

Protein

Fructose-bisphosphate aldolase

Gene

FBA1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei63 – 631Glyceraldehyde 3-phosphateBy similarity
    Active sitei110 – 1101Proton donorBy similarity
    Metal bindingi111 – 1111Zinc 1; catalyticBy similarity
    Metal bindingi145 – 1451Zinc 2By similarity
    Metal bindingi175 – 1751Zinc 2By similarity
    Metal bindingi227 – 2271Zinc 1; catalyticBy similarity
    Binding sitei228 – 2281Dihydroxyacetone phosphate; via amide nitrogenBy similarity
    Metal bindingi266 – 2661Zinc 1; catalyticBy similarity

    GO - Molecular functioni

    1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00183.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase (EC:4.1.2.13)
    Short name:
    FBP aldolase
    Short name:
    FBPA
    Alternative name(s):
    Fructose-1,6-bisphosphate aldolase
    Gene namesi
    Name:FBA1
    Ordered Locus Names:KLLA0E07546g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome E

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 361361Fructose-bisphosphate aldolasePRO_0000178758Add
    BLAST

    Proteomic databases

    PRIDEiQ9C2U0.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi28985.Q9C2U0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C2U0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni267 – 2693Dihydroxyacetone phosphate bindingBy similarity
    Regioni288 – 2914Dihydroxyacetone phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0191.
    HOGENOMiHOG000227794.
    KOiK01624.
    OMAiHNSLDFV.
    OrthoDBiEOG7HTHSN.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR006411. Fruct_bisP_bact.
    IPR000771. Ketose_bisP_aldolase_II.
    [Graphical view]
    PfamiPF01116. F_bP_aldolase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
    TIGRFAMsiTIGR00167. cbbA. 1 hit.
    TIGR01520. FruBisAldo_II_A. 1 hit.
    PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9C2U0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAQDVLTRK TGVIVGDDVK ALFDYAKEHK FAIPAINVTS SSTVVAALEA    50
    ARDNKSPIIL QTSNGGAAYF AGKGVSNEGQ NASIRGSIAA AHYIRSIAPA 100
    YGIPVVLHTD HCAKKLLPWF DGMLKADEEY FAKHGEPLFS SHMLDLSEET 150
    DEENIGLCVK YFTRMAKIHQ WLEMEIGITG GEEDGVNNEG TSNDKLYTTP 200
    ETVFSVHEAL SKISPNFSIA SAFGNVHGVY KIAAALKPEL LGTFQDYAAK 250
    QLNKKAEDKP LYLVFHGGSG SSTKDFHTAI DFGVVKVNLD TDCQFAYLSG 300
    IRDYVLNKKD YLMTPVGNPT GEDSPNKKYY DPRVWVREGE KTMSKRITQA 350
    LEIFRTKGAL E 361
    Length:361
    Mass (Da):39,600
    Last modified:October 1, 2002 - v2
    Checksum:iDCF0BEC26FF953D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ272114 Genomic DNA. Translation: CAC29023.2.
    CR382125 Genomic DNA. Translation: CAG99377.1.
    RefSeqiXP_454290.1. XM_454290.1.

    Genome annotation databases

    GeneIDi2894094.
    KEGGikla:KLLA0E07569g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ272114 Genomic DNA. Translation: CAC29023.2 .
    CR382125 Genomic DNA. Translation: CAG99377.1 .
    RefSeqi XP_454290.1. XM_454290.1.

    3D structure databases

    ProteinModelPortali Q9C2U0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 28985.Q9C2U0.

    Proteomic databases

    PRIDEi Q9C2U0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2894094.
    KEGGi kla:KLLA0E07569g.

    Phylogenomic databases

    eggNOGi COG0191.
    HOGENOMi HOG000227794.
    KOi K01624.
    OMAi HNSLDFV.
    OrthoDBi EOG7HTHSN.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR006411. Fruct_bisP_bact.
    IPR000771. Ketose_bisP_aldolase_II.
    [Graphical view ]
    Pfami PF01116. F_bP_aldolase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001359. F_bP_aldolase_II. 1 hit.
    TIGRFAMsi TIGR00167. cbbA. 1 hit.
    TIGR01520. FruBisAldo_II_A. 1 hit.
    PROSITEi PS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and transcriptional regulation of the Kluyveromyces lactis FBA1 (fructose-1,6-bisphosphate aldolase) gene."
      Diaz Prado S.M., Cerdan M.E., Gonzalez Siso M.I.
      Can. J. Microbiol. 50:645-652(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
    2. "Genome evolution in yeasts."
      Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
      , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
      Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

    Entry informationi

    Entry nameiALF_KLULA
    AccessioniPrimary (citable) accession number: Q9C2U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2004
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 80 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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