ID ACSA_CUPNH Reviewed; 660 AA.
AC P31638; Q0K8Q9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
DE EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
DE AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
DE AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
GN Name=acsA {ECO:0000255|HAMAP-Rule:MF_01123}; Synonyms=acoE;
GN OrderedLocusNames=H16_A2525;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=1356967; DOI=10.1128/jb.174.20.6590-6599.1992;
RA Priefert H., Steinbuechel A.;
RT "Identification and molecular characterization of the acetyl coenzyme A
RT synthetase gene (acoE) of Alcaligenes eutrophus.";
RL J. Bacteriol. 174:6590-6599(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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. Although acetate is the preferred substrate of AcsA,
CC propionate is also used, but at a diminished rate compared with that of
CC acetate. Fatty acids with more than three carbon atoms are usually not
CC accepted as substrates by AcsA. {ECO:0000255|HAMAP-Rule:MF_01123,
CC ECO:0000269|PubMed:1356967}.
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:0000255|HAMAP-
CC Rule:MF_01123};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01123};
CC -!- PATHWAY: Ketone degradation; acetoin degradation.
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000255|HAMAP-Rule:MF_01123}.
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DR EMBL; M97217; AAA21945.1; -; Genomic_DNA.
DR EMBL; AM260479; CAJ93612.1; -; Genomic_DNA.
DR PIR; A45736; A45736.
DR RefSeq; WP_011615709.1; NZ_CP039287.1.
DR AlphaFoldDB; P31638; -.
DR SMR; P31638; -.
DR STRING; 381666.H16_A2525; -.
DR GeneID; 57644651; -.
DR KEGG; reh:H16_A2525; -.
DR PATRIC; fig|381666.6.peg.2916; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_4; -.
DR OrthoDB; 9766486at2; -.
DR BioCyc; MetaCyc:MONOMER-13637; -.
DR UniPathway; UPA00040; -.
DR Proteomes; UP000008210; Chromosome 1.
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:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
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:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..660
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208353"
FT BINDING 197..200
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 317
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 397..399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 421..426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 536
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 555
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT MOD_RES 625
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
SQ SEQUENCE 660 AA; 72602 MW; EA03022F82C5C502 CRC64;
MSAIESVMQE HRVFNPPEGF ASQAAIPSME AYQALCDEAE RDYEGFWARH ARELLHWTKP
FTKVLDQSNA PFYKWFEDGE LNASYNCLDR NLQNGNADKV AIVFEADDGS VTRVTYRELH
GKVCRFANGL KALGIRKGDR VVIYMPMSVE GVVAMQACAR LGATHSVVFG GFSAKSLQER
LVDVGAVALI TADEQMRGGK ALPLKAIADD ALALGGCEAV RNVIVYRRTG GKVAWTEGRD
RWMEDVSAGQ PDTCEAEPVS AEHPLFVLYT SGSTGKPKGV QHSTGGYLLW ALMTMKWTFD
IKPDDLFWCT ADIGWVTGHT YIAYGPLAAG ATQVVFEGVP TYPNAGRFWD MIARHKVSIF
YTAPTAIRSL IKAAEADEKI HPKQYDLSSL RLLGTVGEPI NPEAWMWYYK NIGNERCPIV
DTFWQTETGG HMITPLPGAT PLVPGSCTLP LPGIMAAIVD ETGHDVPNGN GGILVVKRPW
PAMIRTIWGD PERFRKSYFP EELGGKLYLA GDGSIRDKDT GYFTIMGRID DVLNVSGHRM
GTMEIESALV SNPLVAEAAV VGRPDDMTGE AICAFVVLKR SRPTGEEAVK IATELRNWVG
KEIGPIAKPK DIRFGDNLPK TRSGKIMRRL LRSLAKGEEI TQDTSTLENP AILEQLKQAQ
//
