AC   MF_01123;
DC   Protein; auto
TR   HAMAP; MF_01123; -; 1; level=0
XX
Names: Ac_CoA_synth
XX
ID   ACSA
DE   RecName: Full=Acetyl-coenzyme A synthetase;
DE            Short=AcCoA synthetase;
DE            Short=Acs;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase;
DE   AltName: Full=Acyl-activating enzyme;
case <OC:Enterobacterales>
GN   Name=acs;
else
GN   Name=acsA;
end case
XX
case <OC:Enterobacterales>
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC       an essential intermediate at the junction of anabolic and catabolic
CC       pathways. Acs undergoes a two-step reaction. In the first half
CC       reaction, Acs combines acetate with ATP to form acetyl-adenylate
CC       (AcAMP) intermediate. In the second half reaction, it can then transfer
CC       the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the
CC       product AcCoA.
CC   -!- FUNCTION: Enables the cell to use acetate during aerobic growth to
CC       generate energy via the TCA cycle, and biosynthetic compounds via the
CC       glyoxylate shunt. Acetylates CheY, the response regulator involved in
CC       flagellar movement and chemotaxis.
else
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC       an essential intermediate at the junction of anabolic and catabolic
CC       pathways. AcsA undergoes a two-step reaction. In the first half
CC       reaction, AcsA combines acetate with ATP to form acetyl-adenylate
CC       (AcAMP) intermediate. In the second half reaction, it can then transfer
CC       the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the
CC       product AcCoA.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
XX
DR   Pfam; PF00501; AMP-binding; 1; trigger=no
DR   PRINTS; PR00154; AMPBINDING; 1; trigger=no
DR   NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1; trigger=no
DR   PROSITE; PS00455; AMP_BINDING; 1; trigger=no
XX
KW   Acetylation
KW   ATP-binding
KW   Ligase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
XX
GO   GO:0003987; F:acetate-CoA ligase activity
case <OC:Enterobacterales>
GO   GO:0019427; P:acetyl-CoA biosynthetic process from acetate
GO   GO:0006935; P:chemotaxis
end case
XX
FT   From: ACSA_SALTY (Q8ZKF6)
FT   BINDING         387..389
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-[ES]-[PG]
FT   BINDING         411..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [DS]-T-[WF]-W-[QM]-T
FT   BINDING         191..194
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   Condition: [RY]-[AGRKN]-[GSNDP]-x
FT   BINDING         537
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: V
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: [HF]
FT   BINDING         542
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: [IV]
FT   BINDING         311
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   Optional; Condition: [TS]
FT   BINDING         335
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   Optional; Condition: N
FT   BINDING         500
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: D
FT   BINDING         515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: R
FT   BINDING         523
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   Optional; Condition: S
FT   BINDING         526
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: R
FT   BINDING         584
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   Optional; Condition: R
FT   MOD_RES         609
FT                   /note="N6-acetyllysine"
FT   Condition: K
XX
Size: 572-672;
Related: None;
Template: P27550; Q8ZKF6; P9WQD1;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in PSEAE, PSEPK
Plasmid: in AGRRH
Comments: More divergent AcsA present in BACSU is not included in the alignment
XX
# Revision 1.31 2023/06/01
//