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PDBsum entry 3q9c
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of h159a apah complexed with n8-acetylspermidine
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Structure:
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Acetylpolyamine amidohydrolase. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Engineered: yes. Mutation: yes
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Source:
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Mycoplana ramosa. Mycoplana bullata. Organism_taxid: 40837. Gene: apha, aph. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.30Å
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R-factor:
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0.186
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R-free:
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0.227
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Authors:
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P.M.Lombardi,D.W.Christianson
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Key ref:
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P.M.Lombardi
et al.
(2011).
Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases.
Biochemistry,
50,
1808-1817.
PubMed id:
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Date:
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07-Jan-11
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Release date:
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02-Mar-11
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PROCHECK
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Headers
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References
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Q48935
(APAH_MYCRA) -
Acetylpolyamine amidohydrolase from Mycoplana ramosa
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Seq:
Struc:
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341 a.a.
341 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class 1:
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E.C.3.5.1.48
- acetylspermidine deacetylase.
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Reaction:
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N8-acetylspermidine + H2O = spermidine + acetate
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N(8)-acetylspermidine
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+
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H2O
Bound ligand (Het Group name = )
corresponds exactly
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=
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spermidine
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+
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acetate
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Enzyme class 2:
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E.C.3.5.1.62
- acetylputrescine deacetylase.
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Reaction:
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N-acetylputrescine + H2O = putrescine + acetate
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N-acetylputrescine
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+
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H2O
Bound ligand (Het Group name = )
matches with 69.23% similarity
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=
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putrescine
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+
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acetate
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Biochemistry
50:1808-1817
(2011)
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PubMed id:
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Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases.
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P.M.Lombardi,
H.D.Angell,
D.A.Whittington,
E.F.Flynn,
K.R.Rajashankar,
D.W.Christianson.
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ABSTRACT
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