ID Q0FCH9_9RHOB Unreviewed; 645 AA.
AC Q0FCH9;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=acsA {ECO:0000256|HAMAP-Rule:MF_01123};
GN ORFNames=OM2255_11955 {ECO:0000313|EMBL:EAU52070.1};
OS Rhodobacterales bacterium HTCC2255.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU52070.1, ECO:0000313|Proteomes:UP000009381};
RN [1] {ECO:0000313|EMBL:EAU52070.1, ECO:0000313|Proteomes:UP000009381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU52070.1,
RC ECO:0000313|Proteomes:UP000009381};
RA Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-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: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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01123};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-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|HAMAP-Rule:MF_01123}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU52070.1}.
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DR EMBL; AATR01000003; EAU52070.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0FCH9; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_5; -.
DR OrthoDB; 9803968at2; -.
DR BioCyc; RBAC367336:G1GNW-1827-MONOMER; -.
DR Proteomes; UP000009381; Unassembled WGS sequence.
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 CDD; cd05966; ACS; 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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 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:UP000009381}.
FT DOMAIN 23..80
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 82..466
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 528..606
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 190..193
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 307
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 383..385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 407..412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 520
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 536
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 581
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT MOD_RES 606
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ SEQUENCE 645 AA; 71905 MW; 6885CBA15F015EEF CRC64;
MTEKVFQPTP DFAKNAHANK EKYELMYTES VSNPDAFWGE HGKRIDWITP FTKVKNTSFE
YPNISIKWYE DGELNVCENC VDRHLESRGD QTAIIWESDD PNIDKHITYN QLHDHVSRLA
NVYKSLGVGK GDRVILYMPM IPEAAYAMLA CARIGAIHSI VFGGFSPDAL ASRISDCKAS
LVVTADEGPR GGKNIPLKKN VDAALEICGD VKTLVVRRTG NSTPYRENRD FDYEELVSVA
SSDCPVEKMN AEDPLFILYT SGSTGKPKGV VHSSAGYLVY ASMTHQYTFD YQEGDTYWCT
ADVGWITGHS YIVYGPLANG ATTLMFEGTP TYPDASRFWA VCEKHKVNQF YTAPTAIRAL
MGLGDDLVLK HNLSDLRVLG TVGEPINPEA WNWYNEVVGK GVVPIVDTWW QTETGGHMLT
PLPGVTATKP GSATTPFFGV QPVILDSQTG QEIEGACEGV LAIKESWPSQ MRTVYGDHDR
FVKTYFEAYK GYYFTEDGCK RDKDGYYWIT GRVDDVLNVS GHRMGTAEIE SALVAHKDVA
EAAVVGYPHE VKGQGIYCYV TLNASAEYTE ELRTALRGWV RQQIGPIASP DYIQWAPGLP
KTRSGKIMRR ILRKVAENDY NSLGDISTLA EPEVVEKLIE NRMNR
//
