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Overview for MACiE Entry M0224

Version history

General Information

EC Number: 2.3.1.48 (A member of the Transferases, Acyltransferases, Transferring groups other than aminoacyl groups)

Enzyme Name: histone acetyltransferase

Biological Species: Saccharomyces cerevisiae (Baker's Yeast)

Catalytic Chain UniprotKB Accession Codes:

  • Q12341 - Histone acetyltransferase type B catalytic subunit

Representative PDB Code: 1bob - HISTONE ACETYLTRANSFERASE HAT1 FROM SACCHAROMYCESCEREVISIAE IN COMPLEX WITH ACETYL COENZYME A (Resolution = 2.30 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of Acetyl-CoA

Image of Histone

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Image of CoA

Image of Acetylhistone

Acetyl-CoA
C00024
CHEBI:57288
Histone
C01429
CHEBI:15358
CoA
C00010
CHEBI:57287
Acetylhistone
C01997

Overall Comment: After the acetylation of Lys12 of histone H4 the substrate reorientates in the active site and Lys5 of the histone is acetylated using the same residues. There is some structural evidence to suggest that the main chain amide of Phe220 stabilises the oxyanion intermediate. However, the evidence is not sufficient to determine its exact role. The enzyme binds a calcium ion, but this ion is not thought to be catalytic.


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Stepwise Description of the Reaction

Step 1Glu255 deprotonates the Lys12 of the histone substrate, activating it.
Step 2The activated lysine of the histone substrate initiates a nucleophilic addition on acetylCoA.
Step 3The tetrahedral intermediate collapses to form the acetylated histone and activated CoA.
Step 4CoA deprotonates Glu255.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Glu 255 A Side Chain

References

  1. A. Poveda et al. (2008), FEBS Journal, 275, 2122-2136. Site specificity of yeast histone acetyltransferase B complex in vivo.
    Medline: 18373695
  2. M. R. Parthun (2007), Oncogene, 26, 5319-5328. Hat1: the emerging cellular roles of a type B histone acetyltransferase.
    Medline: 17694075
  3. R. C. Trievel et al. (1999), Proc. Natl Acad. Sci. USA, 96, 8931-8936. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator .
    Medline: 10430873
  4. R. N. Dutnall et al. (1998), Cell, 94, 427-438. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily.
    Medline: 9727486

Homologue information for M0224 (1bob)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with the same EC number (different mechanisms):

MACiE Entry Enzyme Name PDB code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0344 histone acetyltransferase 2gtr 0.6666 0.0318 Compare

Compare of the other reactions in MACiE with EC number 2.3.1.48


Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0022 aralkylamine N-acetyltransferase
2.3.1.87
1b6b 3.40.630.30
0.250.0119Compare

Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
histone acetyltransferase complex (cellular component)
histone acetyltransferase activity (molecular function)
protein binding (molecular function)
chromatin silencing at telomere (biological process)
N-acetyltransferase activity (molecular function)
metabolic process (biological process)
chromatin modification (biological process)
histone acetylation (biological process)
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