ID A9MGK6_SALAR Unreviewed; 652 AA.
AC A9MGK6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE Short=AcCoA synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
DE Short=Acs {ECO:0000256|HAMAP-Rule:MF_01123};
DE EC=6.2.1.1 {ECO:0000256|HAMAP-Rule:MF_01123};
DE AltName: Full=Acetate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01123};
DE AltName: Full=Acyl-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01123};
GN Name=acs {ECO:0000256|HAMAP-Rule:MF_01123};
GN OrderedLocusNames=SARI_03400 {ECO:0000313|EMBL:ABX23230.1};
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX23230.1, ECO:0000313|Proteomes:UP000002084};
RN [1] {ECO:0000313|EMBL:ABX23230.1, ECO:0000313|Proteomes:UP000002084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC {ECO:0000313|Proteomes:UP000002084};
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_01123}.
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. {ECO:0000256|HAMAP-Rule:MF_01123}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01123};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01123};
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC activates the enzyme. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|HAMAP-Rule:MF_01123}.
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DR EMBL; CP000880; ABX23230.1; -; Genomic_DNA.
DR AlphaFoldDB; A9MGK6; -.
DR STRING; 41514.SARI_03400; -.
DR KEGG; ses:SARI_03400; -.
DR HOGENOM; CLU_000022_3_6_6; -.
DR Proteomes; UP000002084; Chromosome.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd05966; ACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR HAMAP; MF_01123; Ac_CoA_synth; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF243; ACETYL-COENZYME A SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990, ECO:0000256|HAMAP-
KW Rule:MF_01123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01123};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01123};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01123}; Reference proteome {ECO:0000313|Proteomes:UP000002084}.
FT DOMAIN 24..81
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 83..467
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 531..609
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 191..194
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 311
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 335
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 387..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 411..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 523
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 584
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT MOD_RES 609
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ SEQUENCE 652 AA; 72135 MW; B46FBEF99CE0F8BF CRC64;
MSQTHKHAIP ANVADRCLIN PEQYEAKYQQ SINDPDTFWG EQGKILDWIT PYQKVKNTSF
APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DASQSKHISY RELHRDVCRF
ANTLLDLGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSNS
RLVITADEGI RAGRSIPLKK NVDDALKNPN VTSVEHVIVL KRTGSDIDWQ EDRDLWWRDL
IEKASPEHQP EAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHQ VNILYTAPTA
IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWFWK KIGNEKCPVV DTWWQTETGG
FMITPLPGAT ELKAGSATRP FFGVQPALVD NEGHPQEGAT EGNLVITDSW PGQARTLFGD
HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP
KIAEAAVVGI PHAIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS
//
