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Catalytic Site Atlas Version 2.2.12
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CSA entry for 1f80
Original Entry
Title:
Transferase
Compound:
Acyl carrier protein
Mutant:
No
UniProt/Swiss-Prot:
P80643-ACP_BACSU
P96618-ACPS_BACSU
EC Class:
2.7.8.7
Other CSA Entries:
Overview of all sites for 1f80
Homologues of 1f80
Entries for UniProt/Swiss-Prot: P80643
Entries for UniProt/Swiss-Prot: P96618
Entries for EC: 2.7.8.7
Other Databases:
PDB entry: 1f80
PDBsum entry: 1f80
UniProt/Swiss-Prot: P80643
UniProt/Swiss-Prot: P96618
IntEnz entry: 2.7.8.7
Literature Report:
Introduction:
Holo -(acyl carrier protein) synthase (AcpS) from Bacillus subtilis is of the phosphopantetheinyl transferase superfamily. It catalyses the attachment of the 4'-phosphopantetheinyl moiety of coenzyme A to the sidechain of a serine residue on apo-ACP. AcpS is essential in the initiation of the biosynthesis of fatty acids, polyketide antibiotics and non-ribosomal peptides.
Mechanism:
1. Asp 35 deprotonates a water molecule.
2. This activated water molecule then acts as a general base by deprotonating the substrate serine residue, activating it for nucleophilic attack on the beta-phosphate of CoA.
3. The nucleophilic attack results in the transfer of the phosphopantetheinyl group to the substrate serine residue.
4. The resulting negatively charged 3',5'-ADP is stabilised by interactions with Lys 62, the mainchain amide of His 105 and the magnesium ion.
5. A proton is then transferred to 3',5'-ADP from either a water molecule or Lys 62.
Sites:

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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
1255 0
ElectrostaticSubstrate
Stabilises the negatively charged transition state.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10997907 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
HISA 105 0Backbone amide
ElectrostaticSubstrate
Stabilises the negatively charged intermediate.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10997907 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
LYSC 62 0Sidechain
ElectrostaticSubstrate
Stabilises the negatively charged intermediate. May also act as a proton donor to 3',5'-ADP.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10997907 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ASPF 35 0Sidechain
Acid/baseWater
Deprotonates a water molecule, which in turn deprotonates the substrate serine residue.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10997907 Current protein Residue is positioned appropriately (ligand position known)
Notes:
Lys 62 may also act as a proton donor to 3',5'-ADP, although it could be water which donates this proton.
Na is not 'mutated', it is just present instead of Mg due to the crystallisation process.
References:
1
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
K. D. Parris and L. Lin and A. Tam and R. Mathew and J. Hixon and M. Stahl and C. C. Fritz and J. Seehra and W. S. Somers
Structure 8, (8) 883-95, (2000).
10997907
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