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P00885

- ALKD_PSEPU

UniProt

P00885 - ALKD_PSEPU

Protein

2-dehydro-3-deoxy-phosphogluconate aldolase

Gene

eda

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei61 – 611
    Active sitei145 – 1451Schiff-base intermediate with substrate1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 2-dehydro-3-deoxy-phosphogluconate aldolase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Schiff base

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-dehydro-3-deoxy-phosphogluconate aldolase (EC:4.1.2.14)
    Alternative name(s):
    KDPG-aldolase
    Phospho-2-dehydro-3-deoxygluconate aldolase
    Phospho-2-keto-3-deoxygluconate aldolase
    Gene namesi
    Name:eda
    OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
    Taxonomic identifieri303 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 2262252-dehydro-3-deoxy-phosphogluconate aldolasePRO_0000201035Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.

    Structurei

    Secondary structure

    1
    226
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 2715
    Beta strandi28 – 336
    Helixi38 – 403
    Helixi41 – 5010
    Beta strandi55 – 628
    Helixi65 – 7511
    Beta strandi79 – 846
    Helixi89 – 9810
    Beta strandi101 – 1044
    Helixi110 – 1189
    Helixi130 – 1378
    Turni138 – 1403
    Beta strandi143 – 1464
    Helixi149 – 1524
    Helixi154 – 1629
    Turni163 – 1675
    Beta strandi169 – 1757
    Turni178 – 1803
    Helixi181 – 1866
    Beta strandi193 – 1953
    Helixi201 – 2055
    Helixi209 – 22113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MXSX-ray2.20A2-226[»]
    ProteinModelPortaliP00885.
    SMRiP00885. Positions 11-226.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00885.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the KHG/KDPG aldolase family.Curated

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR000887. Aldlse_KDPG_KHG.
    IPR013785. Aldolase_TIM.
    [Graphical view]
    PfamiPF01081. Aldolase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01182. eda. 1 hit.
    PROSITEiPS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
    PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00885-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTLERPQPK LSMADKAARI DAICEKARIL PVITIAREED ILPLADALAA    50
    GGIRTLEVTL RSQHGLKAIQ VLREQRPELC VGAGTVLDRS MFAAVEAAGA 100
    QFVVTPGITE DILEAGVDSE IPLLPGISTP SEIMMGYALG YRRFKLFPAE 150
    ISGGVAAIKA FGGPFGDIRF CPTGGVNPAN VRNYMALPNV MCVGTGWMLD 200
    SSWIKNGDWA RIEACSAEAI ALLDAN 226
    Length:226
    Mass (Da):24,069
    Last modified:January 23, 2007 - v2
    Checksum:i081FE3492F7A1452
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101E → Q in CAC14910. (PubMed:12393206)Curated
    Sequence conflicti195 – 1962TG → GT in CAC14910. (PubMed:12393206)Curated
    Sequence conflicti220 – 2201I → M in CAC14910. (PubMed:12393206)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ279003 Genomic DNA. Translation: CAC14910.1.
    PIRiA01105. ADPSGP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ279003 Genomic DNA. Translation: CAC14910.1 .
    PIRi A01105. ADPSGP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MXS X-ray 2.20 A 2-226 [» ]
    ProteinModelPortali P00885.
    SMRi P00885. Positions 11-226.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00885.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR000887. Aldlse_KDPG_KHG.
    IPR013785. Aldolase_TIM.
    [Graphical view ]
    Pfami PF01081. Aldolase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01182. eda. 1 hit.
    PROSITEi PS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
    PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the zwf-pgl-eda-operon in Pseudomonas putida strains H and KT2440."
      Petruschka L., Adolf K., Burchhardt G., Dernedde J., Jurgensen J., Herrmann H.
      FEMS Microbiol. Lett. 215:89-95(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: H.
    2. "Complete primary structure of 2-keto-3-deoxy-6-phosphogluconate aldolase."
      Suzuki N., Wood W.A.
      J. Biol. Chem. 255:3427-3435(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-226.
    3. "Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2.8-A resolution."
      Mavridis I.M., Hatada M.H., Tulinsky A., Lebioda L.
      J. Mol. Biol. 162:419-444(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    4. "The folding and quaternary structure of trimeric 2-keto-3-deoxy-6-phosphogluconic aldolase at 3.5-A resolution."
      Mavridis I.M., Tulinsky A.
      Biochemistry 15:4410-4417(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).

    Entry informationi

    Entry nameiALKD_PSEPU
    AccessioniPrimary (citable) accession number: P00885
    Secondary accession number(s): Q9EV78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 80 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

    3D-structure, Direct protein sequencing

    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