ID   ACSA_STRCO              Reviewed;         651 AA.
AC   Q9X928;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 114.
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}; OrderedLocusNames=SCO3563;
GN   ORFNames=SCH5.26;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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. {ECO:0000255|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: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   -!- 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; AL939117; CAB38500.1; -; Genomic_DNA.
DR   PIR; T36684; T36684.
DR   RefSeq; NP_627761.1; NC_003888.3.
DR   RefSeq; WP_003975373.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q9X928; -.
DR   SMR; Q9X928; -.
DR   STRING; 100226.SCO3563; -.
DR   GeneID; 1098999; -.
DR   KEGG; sco:SCO3563; -.
DR   PATRIC; fig|100226.15.peg.3619; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_3_6_11; -.
DR   InParanoid; Q9X928; -.
DR   OMA; AIKASWP; -.
DR   PhylomeDB; Q9X928; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
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:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 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..651
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_0000208389"
FT   BINDING         193..196
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         312
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         388..390
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         412..417
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         501
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         516
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         524
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         538
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         540
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         543
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   MOD_RES         610
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
SQ   SEQUENCE   651 AA;  71045 MW;  3A04CFD3ED436EC5 CRC64;
     MSNESLANLL KEERRFAPPA DLAANANVTA EAYEQAKADR LGFWAEQARR LTWAKEPTET
     LDWSNPPFAK WFKDGTLNVA YNCVDRHVEA GNGDRVAIHF EGESGDSRAL TYAQLKDEVS
     KAANALLELG VQKGDRVAIY MPMIPETAIA MLACARIGAA HSVVFGGFSS DALATRIQDA
     DARVVITADG GYRRGKPSAL KPAVDEAVER AGIVEHVLVV RRTGQDVAWD DSRDKWWHET
     VDGQSAEHTP EAFDAEHPLF ILYTSGTTGK PKGILHTSGG YLTQTAYTHW AVFDLKPETD
     VFWCTADVGW VTGHSYIVYG PLANGATQVM YEGTPDTPHQ GRFWEIVQKY GVTILYTAPT
     AIRTFMKWGD DIPAKFDLSS LRVLGSVGEP INPEAWIWYR KNIGADATPV VDTWWQTETG
     AMMITPLPGV THAKPGSAQR PLPGISATVV DDEANEVPNG GGGYLVLTEP WPSMLRTIWG
     DDQRFIDTYW SRFEGKYFAG DGAKKDDDGD IWLLGRVDDV MLVSGHNIST TEVESALVSH
     PSVAEAAVVG ATDETTGQAI VAFVILRGTT AESEDLVAEL RNHVGATLGP IAKPKRILPV
     SELPKTRSGK IMRRLLRDVA ENRQVGDVTT LADSTVMDLI QTKLPAAPSE D