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P29271

- ALF2_RHOSH

UniProt

P29271 - ALF2_RHOSH

Protein

Fructose-bisphosphate aldolase 2

Gene

cfxB

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      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

    BioCyciRETL1328306-WGS:GSTH-5054-MONOMER.
    UniPathwayiUPA00109; UER00183.
    UPA00116.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase 2 (EC:4.1.2.13)
    Short name:
    FBP aldolase
    Short name:
    FBPA
    Alternative name(s):
    Fructose-1,6-bisphosphate aldolase
    Fructose-bisphosphate aldolase II
    Gene namesi
    Name:cfxB
    OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
    Taxonomic identifieri1063 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Fructose-bisphosphate aldolase 2PRO_0000178733Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    3D structure databases

    ProteinModelPortaliP29271.
    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.

    P29271-1 [UniParc]FASTAAdd to Basket

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    MALITLRQLL DHAAEQGYGV PAFNINNMEQ GLAIMEAARA CDAPVIIQAS    50
    RGARSYANDI MLAKMIEALA AIYPEIPLCM HQDHGNNEAT CMTAIRHGFT 100
    SVMMDGSLKA DAKTPADYDY NVDITARVSH MAHWVGASVE GELGVLGSLE 150
    TGESEAEDGH GAEGKLDHSQ LLTDPDQAVD FVKKTQVDAL AIACGTSHGA 200
    YKFSRKPDGE ILAMSVIEAI HKKLPDTHLV MHGSSSVPQE LQDIINAFGG 250
    AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMAMTGQFRR IAQQTPSEFD 300
    PRKFLKPAMD AMRDLCKQRL EAFGTAGQAG KIRIIPMDDM AKRYASGALA 350
    PKTA 354
    Length:354
    Mass (Da):38,269
    Last modified:December 1, 1992 - v1
    Checksum:i9F547E84FC72ACF5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M68914 Genomic DNA. Translation: AAA26157.1.
    PIRiD41080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M68914 Genomic DNA. Translation: AAA26157.1 .
    PIRi D41080.

    3D structure databases

    ProteinModelPortali P29271.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .
    UPA00116 .
    BioCyci RETL1328306-WGS:GSTH-5054-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. "Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides."
      Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.
      J. Biol. Chem. 266:20447-20452(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiALF2_RHOSH
    AccessioniPrimary (citable) accession number: P29271
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein is encoded within the form II ribulose-bisphosphate carboxylase operon.

    Documents

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

    External Data

    Dasty 3