ID   A3PBZ3_PROM0            Unreviewed;       660 AA.
AC   A3PBZ3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   02-SEP-2026, entry version 106.
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:0000313|EMBL:ABO17268.1};
GN   Synonyms=acsA {ECO:0000256|HAMAP-Rule:MF_01123};
GN   OrderedLocusNames=P9301_06451 {ECO:0000313|EMBL:ABO17268.1};
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO17268.1, ECO:0000313|Proteomes:UP000001430};
RN   [1] {ECO:0000313|EMBL:ABO17268.1, ECO:0000313|Proteomes:UP000001430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO17268.1,
RC   ECO:0000313|Proteomes:UP000001430};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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: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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000131, ECO:0000256|HAMAP-
CC         Rule:MF_01123};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         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|ARBA:ARBA00006432, ECO:0000256|HAMAP-Rule:MF_01123}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01123}.
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DR   EMBL; CP000576; ABO17268.1; -; Genomic_DNA.
DR   RefSeq; WP_011862635.1; NC_009091.1.
DR   AlphaFoldDB; A3PBZ3; -.
DR   STRING; 167546.P9301_06451; -.
DR   KEGG; pmg:P9301_06451; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_3_6_3; -.
DR   OrthoDB; 9778383at2; -.
DR   Proteomes; UP000001430; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0003987; F:acetyl-CoA synthetase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd05966; ACS; 1.
DR   FunFam; 3.40.50.12780:FF:000001; Acetyl-coenzyme A synthetase; 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; IPR045851; AMP-b_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_synth/lig_dom.
DR   InterPro; IPR042099; ANL_N_sf.
DR   NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   NCBIfam; NF001208; PRK00174.1; 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 {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|HAMAP-Rule:MF_01123};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01123}; Reference proteome {ECO:0000313|Proteomes:UP000001430}.
FT   DOMAIN          40..92
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          102..486
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          547..625
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   BINDING         202..205
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         322
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         398..400
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         422..427
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         516
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         531
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         539
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         542
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         553
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         555
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   BINDING         558
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT   MOD_RES         625
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ   SEQUENCE   660 AA;  74035 MW;  8EC977BFDFF2C40D CRC64;
     MTLDKKNSIN NILEEKRIFP PSKKFAENSN ISTQEELLSL KKQASDNPIQ FWESFAKSEL
     DWFEPFQTVL DNENAPFFKW FKEGKLNITY NCLDRHIKRG LGGKTALIWE GEPGDSKKYT
     YEELLKEVCR AANALKAIGV KKGDLVCIYM PMIPEAMFAM LACARIGAPH SVVFGGFSSE
     ALKDRLIDGN ARYVITADGG FRKDKVIELK QAVDAAIENG ADKVVEKVVV VQRTKKNISM
     VDDRDLWWHE LVKDQKDQCE PEIMSSEDRL FILYTSGSTG KPKGVVHTTG GYNLWSHLTF
     KWIFDLKDDD IYWCTADVGW ITGHSYIVYG PLSNGATTLM YEGVPRRSNL GAFWEIVQKY
     KVSIFYTAPT AIRAFMKSGR EIPDKYNLES LRLLGTVGEP INPEAWMWYK DVIGKDKCPI
     VDTWWQTETG GVMISPLPGV VATKPGSATF PLPGIEVEIV DKDGDKVKEN EGGYLIIKKP
     WPGMMRTIHG NSKRYLESYW EYISFKGEKN VYFAGDGARI DEDGYIWIMG RVDDVISVSG
     HRLGTMEIES ALVSHKSVAE SAVVGKKDDL KGEVIVAFVS LEKDVNGSSE LVEDLKKHVV
     NEIGIIAKPE KIIISDSLPK TRSGKIMRRI LRSLAGGEKI SGDISTLEDS SVLEKLKELS
//