ACSA_SACD2
ID ACSA_SACD2 Reviewed; 645 AA.
AC Q21LV0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Sde_1067;
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD80329.1; -; Genomic_DNA.
DR RefSeq; WP_011467549.1; NC_007912.1.
DR AlphaFoldDB; Q21LV0; -.
DR SMR; Q21LV0; -.
DR STRING; 203122.Sde_1067; -.
DR EnsemblBacteria; ABD80329; ABD80329; Sde_1067.
DR KEGG; sde:Sde_1067; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_6; -.
DR OMA; AIKASWP; -.
DR OrthoDB; 141801at2; -.
DR Proteomes; UP000001947; Chromosome.
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; Reference proteome.
FT CHAIN 1..645
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_1000065313"
FT BINDING 190..193
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 308
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 384..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 408..413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 497
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 520
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 536
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 MOD_RES 606
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
SQ SEQUENCE 645 AA; 71126 MW; B6FCBE9971BCF90A CRC64;
MSTPHLYPVP EALAANAHIN NEKYHTDYAR SINEPDVFWA EKAREFLTWD KPWQSVRSFD
FHKGEATWFE GGKLNVTVNC IDRHLPTKAN DVAIIWEGDD PSVDASITYQ QLHDAVCKFA
NVLKARGVAK GDRVCIYMPM IPEAAYAMLA CARIGAVHSI VFGGFSPEAL KDRIVDSDCK
VLITADEGLR GGRAVALKAN ADKAVAHCPQ VHSVIVVKRT GADVAWNTER DIWLHEAQQS
VDTVCEPESM DSEDPLFILY TSGSTGKPKG VLHTTGGYLL QAAMTHKYVF DYQPGEVYWC
TADVGWVTGH TYIVYGPLTN GATTLMFEGV PTYPTAARCW EVCDKHNVNI FYTAPTAIRA
LMGQGDEFVA STQRKSLRIL GTVGEPINPE AWEWYYNVVG DRRCPIMDTW WQTETGGHML
TPLPGAIDLK PGSATLPFFG VEPVLLDGEG NIIEGEGEGS LAIKSSWPGQ IRTVYGDHDR
LIQTYFSTYP GYYFTGDGAR RDADGYYWIT GRVDDVLNVS GHRMGTAEVE SALVLHPKVA
EAAVVGYPHD VKGQGIYAYV TLMTGVEPDD GLRKELVAMC TQEIGPIAKP DLIQWAPGLP
KTRSGKIMRR ILRKVAANEL DTLGDTSTLA DPSVVDDLIE NRMNR
