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P14223

- ALF_PLAFA

UniProt

P14223 - ALF_PLAFA

Protein

Fructose-bisphosphate aldolase

Gene
N/A
Organism
Plasmodium falciparum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621Substrate
    Binding sitei152 – 1521Substrate
    Active sitei195 – 1951Proton acceptorBy similarity
    Active sitei237 – 2371Schiff-base intermediate with dihydroxyacetone-P
    Sitei369 – 3691Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

    GO - Molecular functioni

    1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00183.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase (EC:4.1.2.13)
    Alternative name(s):
    41 kDa antigen
    OrganismiPlasmodium falciparum
    Taxonomic identifieri5833 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 369369Fructose-bisphosphate aldolasePRO_0000216930Add
    BLAST

    Proteomic databases

    PRIDEiP14223.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    DIPiDIP-60915N.

    Structurei

    Secondary structure

    1
    369
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 2914
    Beta strandi35 – 395
    Helixi43 – 5210
    Helixi59 – 7012
    Turni76 – 783
    Beta strandi79 – 846
    Helixi86 – 894
    Helixi99 – 1068
    Beta strandi109 – 1135
    Beta strandi118 – 1203
    Beta strandi124 – 1263
    Beta strandi128 – 1303
    Turni133 – 1353
    Helixi136 – 14611
    Beta strandi150 – 1578
    Helixi161 – 1633
    Helixi168 – 18720
    Beta strandi191 – 1988
    Helixi206 – 22621
    Helixi231 – 2333
    Helixi253 – 26715
    Beta strandi274 – 2774
    Helixi284 – 29613
    Beta strandi301 – 3099
    Helixi310 – 3189
    Turni319 – 3224
    Turni324 – 3263
    Helixi327 – 34620

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A5CX-ray3.00A/B2-369[»]
    2EPHX-ray2.70A/B/C/D1-369[»]
    2PC4X-ray2.40A/B/C/D1-369[»]
    ProteinModelPortaliP14223.
    SMRiP14223. Positions 4-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14223.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3588.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR000741. FBA_I.
    [Graphical view]
    PfamiPF00274. Glycolytic. 1 hit.
    [Graphical view]
    PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14223-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHCTEYMNA PKKLPADVAE ELATTAQKLV QAGKGILAAD ESTQTIKKRF    50
    DNIKLENTIE NRASYRDLLF GTKGLGKFIS GAILFEETLF QKNEAGVPMV 100
    NLLHNENIIP GIKVDKGLVN IPCTDEEKST QGLDGLAERC KEYYKAGARF 150
    AKWRTVLVID TAKGKPTDLS IHETAWGLAR YASICQQNRL VPIVEPEILA 200
    DGPHSIEVCA VVTQKVLSCV FKALQENGVL LEGALLKPNM VTAGYECTAK 250
    TTTQDVGFLT VRTLRRTVPP ALPGVVFLSG GQSEEEASVN LNSINALGPH 300
    PWALTFSYGR ALQASVLNTW QGKKENVAKA REVLLQRAEA NSLATYGKYK 350
    GGAGGENAGA SLYEKKYVY 369
    Length:369
    Mass (Da):40,105
    Last modified:January 1, 1990 - v1
    Checksum:i2AE9CDED4F5C96A4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28881 Genomic DNA. Translation: AAA29473.1.
    A13461 Unassigned DNA. Translation: CAA01107.1.
    A13481 Unassigned DNA. Translation: CAA01117.1.
    PIRiA44942.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M28881 Genomic DNA. Translation: AAA29473.1 .
    A13461 Unassigned DNA. Translation: CAA01107.1 .
    A13481 Unassigned DNA. Translation: CAA01117.1 .
    PIRi A44942.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A5C X-ray 3.00 A/B 2-369 [» ]
    2EPH X-ray 2.70 A/B/C/D 1-369 [» ]
    2PC4 X-ray 2.40 A/B/C/D 1-369 [» ]
    ProteinModelPortali P14223.
    SMRi P14223. Positions 4-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60915N.

    Proteomic databases

    PRIDEi P14223.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG3588.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00183 .

    Miscellaneous databases

    EvolutionaryTracei P14223.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR000741. FBA_I.
    [Graphical view ]
    Pfami PF00274. Glycolytic. 1 hit.
    [Graphical view ]
    PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new blood stage antigen of Plasmodium falciparum transported to the erythrocyte surface."
      Knapp B., Hundt E., Kuepper H.A.
      Mol. Biochem. Parasitol. 37:47-56(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Plasmodium falciparum aldolase: gene structure and localization."
      Knapp B., Hundt E., Kuepper H.A.
      Mol. Biochem. Parasitol. 40:1-12(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum."
      Kim H., Certa U., Dobeli H., Jakob P., Hol W.G.J.
      Biochemistry 37:4388-4396(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

    Entry informationi

    Entry nameiALF_PLAFA
    AccessioniPrimary (citable) accession number: P14223
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3