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Q59101

- ALF2_CUPNH

UniProt

Q59101 - ALF2_CUPNH

Protein

Fructose-bisphosphate aldolase, plasmid

Gene

cbbAP

Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      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 sitei83 – 831Proton donorBy similarity
    Metal bindingi84 – 841Zinc 1; catalyticBy similarity
    Metal bindingi105 – 1051Zinc 2By similarity
    Metal bindingi142 – 1421Zinc 2By similarity
    Metal bindingi198 – 1981Zinc 1; catalyticBy similarity
    Binding sitei199 – 1991Dihydroxyacetone phosphate; via amide nitrogenBy similarity
    Metal bindingi232 – 2321Zinc 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
    2. reductive pentose-phosphate cycle Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Calvin cycle, Glycolysis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciCNEC381666:GJUJ-6690-MONOMER.
    UniPathwayiUPA00109; UER00183.
    UPA00116.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase, plasmid (EC:4.1.2.13)
    Short name:
    FBP aldolase
    Short name:
    FBPA
    Alternative name(s):
    Fructose-1,6-bisphosphate aldolase
    Gene namesi
    Name:cbbAP
    Ordered Locus Names:PHG416
    Encoded oniPlasmid megaplasmid pHG10 Publication
    OrganismiCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha)
    Taxonomic identifieri381666 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000008210: Plasmid megaplasmid pHG1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345Fructose-bisphosphate aldolase, plasmidPRO_0000178728Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi381666.PHG416.

    Structurei

    3D structure databases

    ProteinModelPortaliQ59101.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni233 – 2353Dihydroxyacetone phosphate bindingBy similarity
    Regioni275 – 2784Dihydroxyacetone phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0191.
    HOGENOMiHOG000227792.
    KOiK01624.
    OMAiGHYSHVE.
    OrthoDBiEOG6HXJ7B.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR006412. Fruct_bisP_Calv.
    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.
    TIGR01521. FruBisAldo_II_B. 1 hit.
    PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q59101-1 [UniParc]FASTAAdd to Basket

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    MALISLRQLL DHAGEFGYGV PAFNVNNLEQ IHAIMEAAEE TDSPVILQAS    50
    AGARKYAGEA YLRHMVLAAA ETHPDIPIVL HQDHGSSPAV CQASIRSGFT 100
    SVMMDGSLRE DMKTPSDYDY NVDVTRRVCE MAHAVGVSVE GELGCLGSLE 150
    TGQAGEEDGV GAAGTLSHDM MLTDPAQARD FVARTGVDAL AIAIGTSHGA 200
    YKFSRKPTGD ILAIDRIREI HEQIPDTHLV MHGSSSVPQE WLEIIRQYGG 250
    DIKETYGVPV EEILRGIKTG VRKVNIDTDI RLAMTGAIRK SLAEDRSEFD 300
    PRKALLAAKK GARSVVKLRF EAFGCAGQAS KIKPIAMEQL AQWYR 345
    Length:345
    Mass (Da):37,412
    Last modified:January 4, 2005 - v2
    Checksum:iB5E2CBB6200388B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti285 – 2851T → I in AAC43448. (PubMed:7763137)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12423 Genomic DNA. Translation: AAC43448.1.
    AY305378 Genomic DNA. Translation: AAP86165.1.
    PIRiI39555.
    RefSeqiNP_943051.1. NC_005241.1.

    Genome annotation databases

    EnsemblBacteriaiAAP86165; AAP86165; PHG416.
    GeneIDi2656760.
    KEGGireh:PHG416.
    PATRICi35229344. VBIRalEut6770_0344.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12423 Genomic DNA. Translation: AAC43448.1 .
    AY305378 Genomic DNA. Translation: AAP86165.1 .
    PIRi I39555.
    RefSeqi NP_943051.1. NC_005241.1.

    3D structure databases

    ProteinModelPortali Q59101.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 381666.PHG416.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP86165 ; AAP86165 ; PHG416 .
    GeneIDi 2656760.
    KEGGi reh:PHG416.
    PATRICi 35229344. VBIRalEut6770_0344.

    Phylogenomic databases

    eggNOGi COG0191.
    HOGENOMi HOG000227792.
    KOi K01624.
    OMAi GHYSHVE.
    OrthoDBi EOG6HXJ7B.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    UPA00116 .
    BioCyci CNEC381666:GJUJ-6690-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR006412. Fruct_bisP_Calv.
    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.
    TIGR01521. FruBisAldo_II_B. 1 hit.
    PROSITEi PS00602. ALDOLASE_CLASS_II_1. 1 hit.
    PS00806. ALDOLASE_CLASS_II_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the genes forming the distal parts of the two cbb CO2 fixation operons from Alcaligenes eutrophus."
      Schaeferfohann J., Yoo J.-G., Bowien B.
      Arch. Microbiol. 163:291-299(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."
      Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.
      J. Mol. Biol. 332:369-383(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

    Entry informationi

    Entry nameiALF2_CUPNH
    AccessioniPrimary (citable) accession number: Q59101
    Secondary accession number(s): Q7WWS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 92 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, Plasmid, 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