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Q56815

- ALF_XANFL

UniProt

Q56815 - ALF_XANFL

Protein

Fructose-bisphosphate aldolase

Gene

cbbA

Organism
Xanthobacter flavus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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

    UniPathwayiUPA00109; UER00183.
    UPA00116.

    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:cbbA
    OrganismiXanthobacter flavus
    Taxonomic identifieri281 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Fructose-bisphosphate aldolasePRO_0000178755Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ56815.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    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.

    Q56815-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALVSMRQLL DHAADDSYGL PAFNVNNMEQ VKAIMDAARA TSSPVILQGS    50
    AGARKYAGEP FLRHLIAAAV EAYPEIPVVM HQDHGASPAV CMGAIKSGFS 100
    SVMMDGSLKE DGKTPADYDY NVSVTAKVVE LAHAVGVSVE GELGCLGSLE 150
    TGKGEAEDGH GAEEALDHSK LLTDPDEAAQ FVKATQCDAL AIAIGTSHGA 200
    YKFTRKPTGD ILAIDRIKAI HQRIPTTHLV MHGSSSVPQE LLEEIRTYGG 250
    DIKETYGVPV EEIQEGIRYG VRKVNIDTDI RLAMTAAIRR VGAKNKSEFD 300
    PRKFMAAAME EAKKVCIARF EAFGSAGKAE KIRAIELDEM AKRYASGELA 350
    QVVH 354
    Length:354
    Mass (Da):37,982
    Last modified:November 1, 1996 - v1
    Checksum:iDDF44661B527E4B7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29134 Genomic DNA. Translation: AAA96742.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29134 Genomic DNA. Translation: AAA96742.1 .

    3D structure databases

    ProteinModelPortali Q56815.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    UPA00116 .

    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. "Primary structure and phylogeny of the Calvin cycle enzymes transketolase and fructosebisphosphate aldolase of Xanthobacter flavus."
      van den Bergh E.R., Baker S.C., Raggers R.J., Terpstra P., Woudstra E.C., Dijkhuizen L., Meijer W.G.
      J. Bacteriol. 178:888-893(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: H4-14.

    Entry informationi

    Entry nameiALF_XANFL
    AccessioniPrimary (citable) accession number: Q56815
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3