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P0A991

- ALF1_ECOLI

UniProt

P0A991 - ALF1_ECOLI

Protein

Fructose-bisphosphate aldolase class 1

Gene

fbaB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Enzyme regulationi

    Activated by citrate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei237 – 2371Schiff-base intermediate with dihydroxyacetone-P

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciEcoCyc:FRUCBISALD-CLASSI-MONOMER.
    ECOL316407:JW5344-MONOMER.
    MetaCyc:FRUCBISALD-CLASSI-MONOMER.
    SABIO-RKP0A991.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase class 1 (EC:4.1.2.13)
    Alternative name(s):
    Fructose-bisphosphate aldolase class I
    Short name:
    FBP aldolase
    Gene namesi
    Name:fbaB
    Synonyms:dhnA
    Ordered Locus Names:b2097, JW5344
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG14062. fbaB.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi237 – 2371K → A: Loss of activity.
    Mutagenesisi239 – 2391K → A: No change in activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 350349Fructose-bisphosphate aldolase class 1PRO_0000138939Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei208 – 2081N6-acetyllysine1 Publication
    Modified residuei262 – 2621N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A991.
    PRIDEiP0A991.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A991.

    Interactioni

    Subunit structurei

    Homooctamer or homodecamer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-545269,EBI-545269

    Protein-protein interaction databases

    DIPiDIP-36197N.
    IntActiP0A991. 5 interactions.
    STRINGi511145.b2097.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A991.
    SMRiP0A991. Positions 70-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1830.
    HOGENOMiHOG000224791.
    KOiK11645.
    OMAiQYDQTLY.
    OrthoDBiEOG6JQGZX.
    PhylomeDBiP0A991.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR002915. DeoC/FbaB/lacD_aldolase.
    [Graphical view]
    PfamiPF01791. DeoC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A991-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDIAQLLGK DADNLLQHRC MTIPSDQLYL PGHDYVDRVM IDNNRPPAVL    50
    RNMQTLYNTG RLAGTGYLSI LPVDQGVEHS AGASFAANPL YFDPKNIVEL 100
    AIEAGCNCVA STYGVLASVS RRYAHRIPFL VKLNHNETLS YPNTYDQTLY 150
    ASVEQAFNMG AVAVGATIYF GSEESRRQIE EISAAFERAH ELGMVTVLWA 200
    YLRNSAFKKD GVDYHVSADL TGQANHLAAT IGADIVKQKM AENNGGYKAI 250
    NYGYTDDRVY SKLTSENPID LVRYQLANCY MGRAGLINSG GAAGGETDLS 300
    DAVRTAVINK RAGGMGLILG RKAFKKSMAD GVKLINAVQD VYLDSKITIA 350
    Length:350
    Mass (Da):38,109
    Last modified:January 23, 2007 - v2
    Checksum:i462341BE2459E587
    GO

    Sequence cautioni

    The sequence AAB18249.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti192 – 1921L → V in AAB18249. 1 PublicationCurated
    Sequence conflicti309 – 3091N → I in AAB18249. 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 37979.3 Da from positions 2 - 350. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73760 Genomic DNA. Translation: AAB18249.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC75158.2.
    AP009048 Genomic DNA. Translation: BAE76584.1.
    RefSeqiNP_416600.4. NC_000913.3.
    YP_490337.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75158; AAC75158; b2097.
    BAE76584; BAE76584; BAE76584.
    GeneIDi12932531.
    946632.
    KEGGiecj:Y75_p2059.
    eco:b2097.
    PATRICi32119527. VBIEscCol129921_2174.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73760 Genomic DNA. Translation: AAB18249.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC75158.2 .
    AP009048 Genomic DNA. Translation: BAE76584.1 .
    RefSeqi NP_416600.4. NC_000913.3.
    YP_490337.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0A991.
    SMRi P0A991. Positions 70-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36197N.
    IntActi P0A991. 5 interactions.
    STRINGi 511145.b2097.

    Proteomic databases

    PaxDbi P0A991.
    PRIDEi P0A991.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75158 ; AAC75158 ; b2097 .
    BAE76584 ; BAE76584 ; BAE76584 .
    GeneIDi 12932531.
    946632.
    KEGGi ecj:Y75_p2059.
    eco:b2097.
    PATRICi 32119527. VBIEscCol129921_2174.

    Organism-specific databases

    EchoBASEi EB3815.
    EcoGenei EG14062. fbaB.

    Phylogenomic databases

    eggNOGi COG1830.
    HOGENOMi HOG000224791.
    KOi K11645.
    OMAi QYDQTLY.
    OrthoDBi EOG6JQGZX.
    PhylomeDBi P0A991.

    Enzyme and pathway databases

    BioCyci EcoCyc:FRUCBISALD-CLASSI-MONOMER.
    ECOL316407:JW5344-MONOMER.
    MetaCyc:FRUCBISALD-CLASSI-MONOMER.
    SABIO-RK P0A991.

    Miscellaneous databases

    PROi P0A991.

    Gene expression databases

    Genevestigatori P0A991.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR002915. DeoC/FbaB/lacD_aldolase.
    [Graphical view ]
    Pfami PF01791. DeoC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Close T.J., Choi D.W.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "The dhnA gene of Escherichia coli encodes a class I fructose bisphosphate aldolase."
      Thomson G.J., Howlett G.J., Ashcroft A.E., Berry A.
      Biochem. J. 331:437-445(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION, MASS SPECTROMETRY.
    5. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208 AND LYS-262, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiALF1_ECOLI
    AccessioniPrimary (citable) accession number: P0A991
    Secondary accession number(s): P71295, P76416, Q2MAX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 73 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally (PubMed:9278503) thought to be a dehydrin.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3