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PF09298

    Table of contents
    1. 1. Topsan Members
    2. 2. Summary

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    Resources
    Pfam ID: DUF1969 PDB: 1qcn_A
    Solved by: non-psi Priority Score: 4.6
    Member of this family is in PDB.
    Co-occurence with annotated domain(s) in one architecture.
    HMMER:
      # sequence matches: 529 # architectures: 7 # taxonomy ids:336
    FFAS:
      Top FFAS hit in PDB: "1qcoA, FUMARYLACETOACETATE HYDROLASE" No significant hits in Pfam.
    GRDB:
      Top significant hit (PDB90): "1qcoA, hydrolase ; crystal structure of fumarylacetoacetate hydrolase complexed with fumarate and acetoacetate "
    CATH: CATH Domain E-value CATH Node
      1hyoA01 5.00E-30 2.30.30.230
    FUNFAM (eval=0 ): Putative uncharacterized protein -like
    PUBSERVER:
      Publications(s) found: 328
      Publications(s) meeting filtering criteria: 44
    GeneSilico Metaserver: (Login and password: Jamboree)
    PDBBLAST: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2
    MGENTHREADER: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2
    PRC: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2
    SPARKS: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2
    BLASTP: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2
    HHBLITS: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2
    COMPASS: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2
    CSBLAST: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2
    HHSEARCH: PDB: 1hyo_A SCOP: predicted d.177.1 ECC: 3.7.1.2

    Topsan Members

    Tag pages as 'PF09298' to appear in this list.

    No TOPSAN member(s) found.

    Summary

    This is an N-terminal domain of fumarylacetoacetate hydrolase, whose exact functional role is unknown. It is structuraly similar to N-terminal domains in 3lzk, aromatic amino acid degradation protein solved by MCSG. Also many other hydrolases, annotates usually as fumarylacetoacetate or 2-keto-4-pentenoate hydratases have this domain. This similarity is not recognized by any of the distant homology recognition programs.

    3lzk_Ndomain.png

     The occurrence of HT1-associated mutations within this domain and in the N-C interdomain interface suggests its minimal structural requirement, although a regulatory function is conceivable given the contacts to the C-terminal beta-roll.

    This domain will be renamed in the Pfam to "FAA_hydrolase_N" or "FAAH_N".

    Reviews

    References

     

    No references found.

    Tag page

    Files (1)

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    153.43 kB17:25, 24 Jan 2012adamActions
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