HAMAP logo
Due to maintenance work, this service will be unavailable from Mon Nov 11 17:30 until Tue Nov 12 09:00 CET. Apologies for the inconvenience.

HAMAP rule MF_01123

Send feedback

General rule information [?]

Accession MF_01123
Dates 24-SEP-2003 (Created)
1-JUN-2023 (Last updated, Version 31)
Name Ac_CoA_synth
Scope(s) Bacteria
Archaea
Template(s) P27550 (ACSA_ECOLI); Q8ZKF6 (ACSA_SALTY); P9WQD1 (ACSA_MYCTU); [ Recover all ]
Triggered by HAMAP; MF_01123 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier ACSA
Protein name RecName: Full=Acetyl-coenzyme A synthetase;
                 Short=AcCoA synthetase;
                 Short=Acs;
                 EC=6.2.1.1;
AltName: Full=Acetate--CoA ligase;
AltName: Full=Acyl-activating enzyme;
case <OC:Enterobacterales>
Gene name Name=acs;
else
Gene name Name=acsA;
end case

Comments [?]

case <OC:Enterobacterales>
FUNCTIONCatalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
FUNCTIONEnables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis.
else
FUNCTIONCatalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
end case
CATALYTIC ACTIVITY Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; EC=6.2.1.1;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
PTMAcetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
SIMILARITYBelongs to the ATP-dependent AMP-binding enzyme family.

Keywords [?]

Acetylation
ATP-binding
Ligase
Magnesium
Metal-binding
Nucleotide-binding

Gene Ontology [?]

GO:0003987; Molecular function:acetate-CoA ligase activity
case <OCellular component:Enterobacterales>
GO:0019427; Biological process:acetyl-CoA biosynthetic process from acetate
GO:0006935; Biological process:chemotaxis
end case

Cross-references [?]

Pfam PF00501; AMP-binding; 1;
PRINTS PR00154; AMPBINDING; 1;
NCBIfam TIGR02188; Ac_CoA_lig_AcsA; 1;
PROSITE PS00455; AMP_BINDING; 1;

Features [?]

From: ACSA_SALTY (Q8ZKF6)
Key From To Description Tag Condition FTGroup
BINDING 387 389 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G-[ES]-[PG]
BINDING 411 416 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [DS]-T-[WF]-W-[QM]-T
BINDING 191 194 /ligand="CoA"
/ligand_id="ChEBI:CHEBI:57287"		 [RY]-[AGRKN]-[GSNDP]-x
BINDING 537 537 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 V
BINDING 539 539 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 [HF]
BINDING 542 542 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 [IV]
BINDING 311 311 /ligand="CoA"
/ligand_id="ChEBI:CHEBI:57287"		 [TS]
BINDING 335 335 /ligand="CoA"
/ligand_id="ChEBI:CHEBI:57287"		 N
BINDING 500 500 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 D
BINDING 515 515 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 R
BINDING 523 523 /ligand="CoA"
/ligand_id="ChEBI:CHEBI:57287"		 S
BINDING 526 526 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 R
BINDING 584 584 /ligand="CoA"
/ligand_id="ChEBI:CHEBI:57287"		 R
MOD_RES 609 609 /note="N6-acetyllysine" K

Additional information [?]

Size range 572-672 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments More divergent AcsA present in BACSU is not included in the alignment



View rule in raw text format (no links)