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P13243

- ALF_BACSU

UniProt

P13243 - ALF_BACSU

Protein

Probable fructose-bisphosphate aldolase

Gene

fbaA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      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 sitei50 – 501Glyceraldehyde 3-phosphateBy similarity
    Active sitei85 – 851Proton donorBy similarity
    Metal bindingi86 – 861Zinc 1; catalyticBy similarity
    Metal bindingi107 – 1071Zinc 2By similarity
    Metal bindingi137 – 1371Zinc 2By similarity
    Metal bindingi181 – 1811Zinc 1; catalyticBy similarity
    Binding sitei182 – 1821Dihydroxyacetone phosphate; via amide nitrogenBy similarity
    Metal bindingi209 – 2091Zinc 1; catalyticBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. fructose 1,6-bisphosphate metabolic process Source: InterPro
    2. glycolytic process Source: UniProtKB-UniPathway
    3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis, Sporulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciBSUB:BSU37120-MONOMER.
    SABIO-RKP13243.
    UniPathwayiUPA00109; UER00183.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable 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:fbaA
    Synonyms:fba, fba1, tsr
    Ordered Locus Names:BSU37120
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU37120. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 285285Probable fructose-bisphosphate aldolasePRO_0000178705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei212 – 2121Phosphothreonine2 Publications
    Modified residuei234 – 2341Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated during sporulation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP13243.

    PTM databases

    PhosSiteiP0802211.

    Interactioni

    Protein-protein interaction databases

    IntActiP13243. 1 interaction.
    MINTiMINT-8365567.
    STRINGi224308.BSU37120.

    Structurei

    3D structure databases

    ProteinModelPortaliP13243.
    SMRiP13243. Positions 1-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni210 – 2123Dihydroxyacetone phosphate bindingBy similarity
    Regioni231 – 2344Dihydroxyacetone phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0191.
    HOGENOMiHOG000227793.
    KOiK01624.
    OMAiCTTRYEA.
    OrthoDBiEOG6HXJ7B.
    PhylomeDBiP13243.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR011289. Fruc_bis_ald_class-2.
    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.
    TIGR01859. fruc_bis_ald_. 1 hit.
    PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P13243-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLVSMTEML NTAKEKGYAV GQFNLNNLEF TQAILQAAEE EKSPVILGVS    50
    EGAGRYMGGF KTVVAMVKAL MEEYKVTVPV AIHLDHGSSF ESCAKAIHAG 100
    FTSVMIDASH HPFEENVATT AKVVELAHFH GVSVEAELGT VGGQEDDVIA 150
    EGVIYADPKE CQELVERTGI DCLAPALGSV HGPYKGEPNL GFKEMEEIGK 200
    STGLPLVLHG GTGIPTADIK KSISLGTAKI NVNTENQISS AKAVRETLAA 250
    KPDEYDPRKY LGPAREAIKE TVIGKMREFG SSNQA 285
    Length:285
    Mass (Da):30,401
    Last modified:June 1, 1994 - v2
    Checksum:i482D3CE048583BCF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22039 Unassigned DNA. Translation: AAA16803.1.
    S42590 Genomic DNA. Translation: AAB22716.1.
    Z49782 Genomic DNA. Translation: CAA89873.1.
    AL009126 Genomic DNA. Translation: CAB15729.1.
    PIRiS55426. D32354.
    RefSeqiNP_391593.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15729; CAB15729; BSU37120.
    GeneIDi937040.
    KEGGibsu:BSU37120.
    PATRICi18979460. VBIBacSub10457_3892.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22039 Unassigned DNA. Translation: AAA16803.1 .
    S42590 Genomic DNA. Translation: AAB22716.1 .
    Z49782 Genomic DNA. Translation: CAA89873.1 .
    AL009126 Genomic DNA. Translation: CAB15729.1 .
    PIRi S55426. D32354.
    RefSeqi NP_391593.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P13243.
    SMRi P13243. Positions 1-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P13243. 1 interaction.
    MINTi MINT-8365567.
    STRINGi 224308.BSU37120.

    PTM databases

    PhosSitei P0802211.

    Proteomic databases

    PaxDbi P13243.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15729 ; CAB15729 ; BSU37120 .
    GeneIDi 937040.
    KEGGi bsu:BSU37120.
    PATRICi 18979460. VBIBacSub10457_3892.

    Organism-specific databases

    GenoListi BSU37120. [Micado ]

    Phylogenomic databases

    eggNOGi COG0191.
    HOGENOMi HOG000227793.
    KOi K01624.
    OMAi CTTRYEA.
    OrthoDBi EOG6HXJ7B.
    PhylomeDBi P13243.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    BioCyci BSUB:BSU37120-MONOMER.
    SABIO-RK P13243.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR011289. Fruc_bis_ald_class-2.
    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.
    TIGR01859. fruc_bis_ald_. 1 hit.
    PROSITEi PS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome."
      Trach K., Chapman J.W., Piggot P.J., Lecoq D., Hoch J.A.
      J. Bacteriol. 170:4194-4208(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    2. "The amino acid sequence of a Bacillus subtilis phosphoprotein that matches an orfY-tsr coding sequence."
      Mitchell C., Morris P.W., Lum L., Spiegelman G., Vary J.C.
      Mol. Microbiol. 6:1345-1349(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26, SEQUENCE REVISION.
      Strain: 168 / JH642.
    3. "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
      Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
      Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    4. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    5. "Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis."
      Mitchell C., Morris P.W., Vary J.C.
      J. Bacteriol. 174:2474-2477(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-16, PHOSPHORYLATION.
    6. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
      Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
      Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212 AND THR-234, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.

    Entry informationi

    Entry nameiALF_BACSU
    AccessioniPrimary (citable) accession number: P13243
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3