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P58315

- ALF1_THETK

UniProt

P58315 - ALF1_THETK

Protein

Fructose-bisphosphate aldolase class 1

Gene

fba

Organism
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (18 Oct 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).

    Catalytic activityi

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

    Enzyme regulationi

    Activated by citrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei29 – 291Substrate
    Binding sitei33 – 331Substrate
    Binding sitei144 – 1441Substrate
    Active sitei146 – 1461Proton donor
    Binding sitei148 – 1481Substrate
    Active sitei177 – 1771Schiff-base intermediate with dihydroxyacetone-P

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciTTEN768679:GJSY-1253-MONOMER.
    SABIO-RKP58315.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase class 1 (EC:4.1.2.13)
    Alternative name(s):
    Fructose-bisphosphate aldolase class I
    Short name:
    FBP aldolase
    Short name:
    FBPA
    Gene namesi
    Name:fba
    Ordered Locus Names:TTX_1278
    OrganismiThermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
    Taxonomic identifieri768679 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus
    ProteomesiUP000002654: Chromosome

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi144 – 1441W → E: Loss of FBP aldolase activity; when associated with F-146. 1 Publication
    Mutagenesisi146 – 1461Y → F: The catalytic activity is at least 3-fold lower than for the wild-type. Loss of FBP aldolase activity; when associated with E-144. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 263263Fructose-bisphosphate aldolase class 1PRO_0000138952Add
    BLAST

    Interactioni

    Subunit structurei

    Homodecamer (dimer of pentamers).3 Publications

    Structurei

    Secondary structure

    1
    263
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 129
    Beta strandi16 – 227
    Helixi25 – 284
    Helixi31 – 344
    Beta strandi35 – 373
    Helixi38 – 414
    Helixi43 – 5311
    Beta strandi56 – 605
    Helixi62 – 687
    Beta strandi71 – 733
    Beta strandi75 – 784
    Beta strandi93 – 964
    Helixi98 – 1036
    Beta strandi107 – 1137
    Helixi120 – 13718
    Beta strandi141 – 1455
    Helixi158 – 17114
    Beta strandi174 – 1796
    Helixi184 – 19310
    Turni194 – 1963
    Beta strandi199 – 2024
    Helixi210 – 22213
    Beta strandi227 – 2315
    Helixi232 – 2354
    Helixi240 – 25112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OJXX-ray1.90A/B/C/D/E/F/G/H/I/J1-263[»]
    1OK4X-ray2.10A/B/C/D/E/F/G/H/I/J1-263[»]
    1OK6X-ray2.40A/B/C/D/E/F/G/H/I/J1-263[»]
    1W8SX-ray1.85A/B/C/D/E/F/G/H/I/J1-263[»]
    2YCEX-ray1.93A/B/C/D/E/F/G/H/I/J1-263[»]
    ProteinModelPortaliP58315.
    SMRiP58315. Positions 2-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP58315.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 252Substrate binding
    Regioni177 – 1793Substrate binding
    Regioni202 – 2043Substrate binding
    Regioni231 – 2322Substrate binding

    Sequence similaritiesi

    Belongs to the DeoC/FbaB aldolase family.Curated

    Phylogenomic databases

    KOiK11645.
    OMAiEWKMFEE.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR002915. DeoC/FbaB/lacD_aldolase.
    [Graphical view]
    PfamiPF01791. DeoC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P58315-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANLTEKFLR IFARRGKSII LAYDHGIEHG PADFMDNPDS ADPEYILRLA    50
    RDAGFDGVVF QRGIAEKYYD GSVPLILKLN GKTTLYNGEP VSVANCSVEE 100
    AVSLGASAVG YTIYPGSGFE WKMFEELARI KRDAVKFDLP LVVWSYPRGG 150
    KVVNETAPEI VAYAARIALE LGADAMKIKY TGDPKTFSWA VKVAGKVPVL 200
    MSGGPKTKTE EDFLKQVEGV LEAGALGIAV GRNVWQRRDA LKFARALAEL 250
    VYGGKKLAEP LNV 263
    Length:263
    Mass (Da):28,705
    Last modified:October 18, 2001 - v1
    Checksum:i1399A6D0CF4F0D9E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ310483 Genomic DNA. Translation: CAC48235.1.
    FN869859 Genomic DNA. Translation: CCC81912.1.
    RefSeqiWP_014127167.1. NC_016070.1.
    YP_004892990.1. NC_016070.1.

    Genome annotation databases

    EnsemblBacteriaiCCC81912; CCC81912; TTX_1278.
    GeneIDi11262157.
    KEGGittn:TTX_1278.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ310483 Genomic DNA. Translation: CAC48235.1 .
    FN869859 Genomic DNA. Translation: CCC81912.1 .
    RefSeqi WP_014127167.1. NC_016070.1.
    YP_004892990.1. NC_016070.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OJX X-ray 1.90 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
    1OK4 X-ray 2.10 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
    1OK6 X-ray 2.40 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
    1W8S X-ray 1.85 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
    2YCE X-ray 1.93 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
    ProteinModelPortali P58315.
    SMRi P58315. Positions 2-255.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCC81912 ; CCC81912 ; TTX_1278 .
    GeneIDi 11262157.
    KEGGi ttn:TTX_1278.

    Phylogenomic databases

    KOi K11645.
    OMAi EWKMFEE.

    Enzyme and pathway databases

    BioCyci TTEN768679:GJSY-1253-MONOMER.
    SABIO-RK P58315.

    Miscellaneous databases

    EvolutionaryTracei P58315.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR002915. DeoC/FbaB/lacD_aldolase.
    [Graphical view ]
    Pfami PF01791. DeoC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038992. Aldolase_Ia. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolases."
      Siebers B., Brinkmann H., Doerr C., Tjaden B., Lilie H., van der Oost J., Verhees C.H.
      J. Biol. Chem. 276:28710-28718(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
      Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
    3. "Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins."
      Lorentzen E., Pohl E., Zwart P., Stark A., Russell R.B., Knura T., Hensel R., Siebers B.
      J. Biol. Chem. 278:47253-47260(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
    4. "Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates."
      Lorentzen E., Siebers B., Hensel R., Pohl E.
      Biochemistry 44:4222-4229(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT GLU-144 AND PHE-146 IN COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF TRP-144 AND TYR-146, REACTION MECHANISM, SUBUNIT.

    Entry informationi

    Entry nameiALF1_THETK
    AccessioniPrimary (citable) accession number: P58315
    Secondary accession number(s): G4RK17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 61 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3