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ACSA_SHESM
ID   ACSA_SHESM              Reviewed;         650 AA.
AC   Q0HHN4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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};
GN   OrderedLocusNames=Shewmr4_2362;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-2006) 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. 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; CP000446; ABI39433.1; -; Genomic_DNA.
DR   RefSeq; WP_011623123.1; NC_008321.1.
DR   AlphaFoldDB; Q0HHN4; -.
DR   SMR; Q0HHN4; -.
DR   KEGG; she:Shewmr4_2362; -.
DR   HOGENOM; CLU_000022_3_6_6; -.
DR   OMA; DHWWHDL; -.
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: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.
FT   CHAIN           1..650
FT                   /note="Acetyl-coenzyme A synthetase"
FT                   /id="PRO_1000065323"
FT   BINDING         191..194
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         311
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         335
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         387..389
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         411..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         500
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         523
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         526
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         537
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         542
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   BINDING         584
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT   MOD_RES         609
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
SQ   SEQUENCE   650 AA;  72371 MW;  F55A288D7933FB05 CRC64;
     MSSQSLYKVS GNIAANALVN NDQYKKMYQE SIVNPEGFWR EHGKRIDWIK PYTKIKKTSF
     DDHNLSINWF YDGTLNASAN CLDRHLAEHS DRVAIIWEGD NASEQRKITY GELHTQVCKF
     ANALRSQGVR RGDIVTIYMP MVPEAAVAML ACARIGAVHS VVFGGFSPDS IASRVIDGKS
     KVVITADEGM RGGRAIPLKR NIDDALKHPD VTSVEKVIVL KRTGGKVDWI EGRDVWWHSL
     VETASEHCAV EEMGAEDPLF LLYTSGSTGN PKGVLHTTGG YMVYASMTHE YVFDYKPGEI
     YWCTADVGWI TGHSYMVYGP LANGATVLIH EGIPNHPSPA RLGEMIDRHK VNILYTAPTL
     IRALMAEGKQ HFDKYDGSSL RIMGSVGEPI NPEAWRWYHE VIGHEHCPIV DTWWQTETGG
     ILITPLPGAT DTKPGSATRP FFGVQPALVD NMGNILEGAT EGNLVLLDSW PGQMRTVYGD
     HERFVLTYFK TFRGMYFTGD GARRDEDGYY WITGRVDDVI NVSGHRLGTA EVESALVSHE
     LVAEAAVVGY PHDIKGQGIY AYVTLTRGTE ESEELRQELR QWVRKEIGAL ATPDLIQWAT
     GLPKTRSGKI MRRFLRKIAA NEVTNLGDAS TLADPAVIET LIETRLNRNE
 
 
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