ACSA_PRB01
ID ACSA_PRB01 Reviewed; 641 AA.
AC Q9F7R5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 66.
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};
OS Gamma-proteobacterium EBAC31A08.
OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples.
OX NCBI_TaxID=133804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10988064; DOI=10.1126/science.289.5486.1902;
RA Beja O., Aravind L., Koonin E.V., Suzuki M.T., Hadd A., Nguyen L.P.,
RA Jovanovich S.B., Gates C.M., Feldman R.A., Spudich J.L., Spudich E.N.,
RA DeLong E.F.;
RT "Bacterial rhodopsin: evidence for a new type of phototrophy in the sea.";
RL Science 289:1902-1906(2000).
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; AF279106; AAG10454.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F7R5; -.
DR SMR; Q9F7R5; -.
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..641
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208373"
FT BINDING 186..189
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 304
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 380..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 404..409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 516
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT MOD_RES 602
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
SQ SEQUENCE 641 AA; 71602 MW; 089C618E3867CE28 CRC64;
MPRKLYSPKH SSNPYIKDFD EYKELYKQSI EDPSKFFKNL ANENISWMED FKTTFNNQFN
NAKWFEGGKT NISLNCIDRH LENDPNKIAL IWEGDDPADS KELTYKELHD EVCKFANVLK
DLGVQKGSRV CIYMPMIIET AFAMLACTRI GAVHSVVFGG FSPESLKDRI LDADCKIVIT
ADEGLRGGKK VPLKSNVDEA LLGCPDVKNT LVIKRTGGEI NWDDKKDVWY EDLVKDVSNK
CAPEPMDSED PLFILYTSGS TGKPKGVLHT TAGYLLGAHI SFKYLFGIRP EDKYWCTADV
GWITGHTYIL YGPLSNGATT LMFEGVPTYP SASRCWEICD KHDISIFYTA PTAIRALMAQ
GDDPVKKTKR DSLRILGTVG EPINPEAWDW YYSVVGKSNC EVIDTWWQTE TGSVLISPIA
GITPTKPGSA TLPFFGVKPS LYDEHGNTLE GSNAGNLVIE QSWPSQIRSI YGDHQRMIDT
YFGMYKDIYF TGDGARRDED GYFWITGRVD DVLNVSGHRL GTAEIESALV LHPKIAEAAV
VGFDHPIKGQ GIYAFVTLMI NESFDDNFSY ELKQFVAKEI GAIAKPDLIQ NAPGLPKTRS
GKIMRRILRK IAENDLSNLG DTTTLADPSV VESLIENKQS L
