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P14540

- ALF_YEAST

UniProt

P14540 - ALF_YEAST

Protein

Fructose-bisphosphate aldolase

Gene

FBA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 bindingi265 – 2651Zinc 1; catalyticBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. gluconeogenesis Source: SGD
    2. glycolytic process Source: SGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YKL060C-MONOMER.
    SABIO-RKP14540.
    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:YKL060C
    ORF Names:YKL320
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    SGDiS000001543. FBA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. mitochondrion Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 359358Fructose-bisphosphate aldolasePRO_0000178762Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphothreonine2 Publications
    Modified residuei56 – 561Phosphoserine1 Publication
    Modified residuei63 – 631Phosphoserine1 Publication
    Modified residuei76 – 761Phosphoserine2 Publications
    Modified residuei83 – 831Phosphoserine1 Publication
    Modified residuei96 – 961Phosphoserine1 Publication
    Modified residuei147 – 1471Phosphoserine2 Publications
    Modified residuei150 – 1501Phosphothreonine2 Publications
    Modified residuei179 – 1791Phosphothreonine1 Publication
    Modified residuei268 – 2681Phosphoserine1 Publication
    Modified residuei290 – 2901Phosphothreonine2 Publications
    Modified residuei310 – 3101Phosphotyrosine1 Publication
    Modified residuei313 – 3131Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP14540.
    PaxDbiP14540.
    PeptideAtlasiP14540.

    2D gel databases

    COMPLUYEAST-2DPAGEP14540.
    SWISS-2DPAGEP14540.
    UCD-2DPAGEP14540.

    Expressioni

    Gene expression databases

    GenevestigatoriP14540.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi34073. 96 interactions.
    DIPiDIP-4702N.
    IntActiP14540. 36 interactions.
    MINTiMINT-8285308.
    STRINGi4932.YKL060C.

    Structurei

    3D structure databases

    ProteinModelPortaliP14540.
    SMRiP14540. Positions 10-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni266 – 2683Dihydroxyacetone phosphate bindingBy similarity
    Regioni287 – 2904Dihydroxyacetone phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0191.
    HOGENOMiHOG000227794.
    KOiK01624.
    OMAiCNDLHSA.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14540-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVEQILKRK TGVIVGEDVH NLFTYAKEHK FAIPAINVTS SSTAVAALEA    50
    ARDSKSPIIL QTSNGGAAYF AGKGISNEGQ NASIKGAIAA AHYIRSIAPA 100
    YGIPVVLHSD HCAKKLLPWF DGMLEADEAY FKEHGEPLFS SHMLDLSEET 150
    DEENISTCVK YFKRMAAMDQ WLEMEIGITG GEEDGVNNEN ADKEDLYTKP 200
    EQVYNVYKAL HPISPNFSIA AAFGNCHGLY AGDIALRPEI LAEHQKYTRE 250
    QVGCKEEKPL FLVFHGGSGS TVQEFHTGID NGVVKVNLDT DCQYAYLTGI 300
    RDYVLNKKDY IMSPVGNPEG PEKPNKKFFD PRVWVREGEK TMGAKITKSL 350
    ETFRTTNTL 359
    Length:359
    Mass (Da):39,621
    Last modified:January 23, 2007 - v3
    Checksum:iC67E61BA5C7E8E4C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15003 Genomic DNA. Translation: CAA33111.1.
    Z28060 Genomic DNA. Translation: CAA81897.1.
    X75781 Genomic DNA. Translation: CAA53412.1.
    M32026 Genomic DNA. No translation available.
    BK006944 Genomic DNA. Translation: DAA09097.1.
    PIRiS07855. ADBY2.
    RefSeqiNP_012863.1. NM_001179626.1.

    Genome annotation databases

    EnsemblFungiiYKL060C; YKL060C; YKL060C.
    GeneIDi853805.
    KEGGisce:YKL060C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15003 Genomic DNA. Translation: CAA33111.1 .
    Z28060 Genomic DNA. Translation: CAA81897.1 .
    X75781 Genomic DNA. Translation: CAA53412.1 .
    M32026 Genomic DNA. No translation available.
    BK006944 Genomic DNA. Translation: DAA09097.1 .
    PIRi S07855. ADBY2.
    RefSeqi NP_012863.1. NM_001179626.1.

    3D structure databases

    ProteinModelPortali P14540.
    SMRi P14540. Positions 10-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34073. 96 interactions.
    DIPi DIP-4702N.
    IntActi P14540. 36 interactions.
    MINTi MINT-8285308.
    STRINGi 4932.YKL060C.

    2D gel databases

    COMPLUYEAST-2DPAGE P14540.
    SWISS-2DPAGE P14540.
    UCD-2DPAGE P14540.

    Proteomic databases

    MaxQBi P14540.
    PaxDbi P14540.
    PeptideAtlasi P14540.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL060C ; YKL060C ; YKL060C .
    GeneIDi 853805.
    KEGGi sce:YKL060C.

    Organism-specific databases

    SGDi S000001543. FBA1.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    BioCyci YEAST:YKL060C-MONOMER.
    SABIO-RK P14540.

    Miscellaneous databases

    NextBioi 974960.
    PROi P14540.

    Gene expression databases

    Genevestigatori P14540.

    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. "Molecular cloning, primary structure and disruption of the structural gene of aldolase from Saccharomyces cerevisiae."
      Schwelberger H.G., Kohlwein S.D., Paltauf F.
      Eur. J. Biochem. 180:301-308(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and TOA2 genes, an open reading frame (ORF) similar to a translationally controlled tumour protein, one ORF containing motifs also found in plant storage proteins and 13 ORFs with weak or no homology to known proteins."
      Rasmussen S.W.
      Yeast 10:S63-S68(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Cloning of Saccharomyces cerevisiae promoters using a probe vector based on phleomycin resistance."
      Gatignol A., Dassain M., Tiraby G.
      Gene 91:35-41(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
    6. Jack R.S.
      Thesis (1973), University of Cambridge, United Kingdom
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-40.
    7. Cited for: PROTEIN SEQUENCE OF 333-339.
      Strain: ATCC 204508 / S288c.
    8. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
      Norbeck J., Blomberg A.
      FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
      Strain: ATCC 38531 / Y41.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; THR-150; TYR-310 AND SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-147; THR-179 AND SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-96; SER-147; THR-150; THR-290 AND SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-63; SER-76; SER-83; THR-290 AND SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiALF_YEAST
    AccessioniPrimary (citable) accession number: P14540
    Secondary accession number(s): D6VXM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 144 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1020000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3