ID ACSA_BRADU Reviewed; 648 AA.
AC Q89WV5; Q93Q03;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 27-MAR-2024, entry version 107.
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=blr0573;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-605, AND MUTAGENESIS OF GLY-263;
RP GLY-266; LYS-269 AND GLU-414.
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=11726281; DOI=10.1093/oxfordjournals.jbchem.a003052;
RA Lee H.Y., Na K.B., Koo H.M., Kim Y.S.;
RT "Identification of active site residues in Bradyrhizobium japonicum acetyl-
RT CoA synthetase.";
RL J. Biochem. 130:807-813(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK95494.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BA000040; BAC45838.1; -; Genomic_DNA.
DR EMBL; AF290478; AAK95494.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; NP_767213.1; NC_004463.1.
DR RefSeq; WP_028174953.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89WV5; -.
DR SMR; Q89WV5; -.
DR STRING; 224911.AAV28_42145; -.
DR EnsemblBacteria; BAC45838; BAC45838; BAC45838.
DR GeneID; 64020436; -.
DR KEGG; bja:blr0573; -.
DR PATRIC; fig|224911.44.peg.9115; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_5; -.
DR InParanoid; Q89WV5; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
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:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..648
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208355"
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 332
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 BINDING 581
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT MOD_RES 606
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT MUTAGEN 263
FT /note="G->I: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11726281"
FT MUTAGEN 266
FT /note="G->I: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:11726281"
FT MUTAGEN 269
FT /note="K->G: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:11726281"
FT MUTAGEN 414
FT /note="E->Q: Great decrease in activity."
FT /evidence="ECO:0000269|PubMed:11726281"
SQ SEQUENCE 648 AA; 72030 MW; 4D439C3AF01483B0 CRC64;
MSEKIYDVPA EWAKRAWVDQ AKYKEMYARS ISDPNGFWAE QAKRIDWMKA PTKIENVSFA
PGNVSIKWFE DGVLNVAHNC IDRHLHKRAN QTAIIWEGDD PSQSRHITYK ELHDEVCRMA
NILRTRNVKK GDRVTIYLPM IPEAAYAMLA CARIGAIHSV VFAGFSPDSL AQRINDCQSK
VIITADEGLR GGKKVPLKAN VDAALAKADG VDWVVVVKRT GGKIDMNPTR DLWYHEAAAM
VTTECPVEHM HAEDPLFILY TSGSTGQPKG VLHTSAGYLV YAAMTHQYVF DYHDGDIYWC
TADVGWVTGH SYILYGPLAN GATTLMFEGV PNYPDNSRFW NVIDKHKVNT FYTAPTAIRA
LMQGGDEPVK KTSRASLRLL GSVGEPINPE AWEWYHRVVG EDRCPIVDTW WQTETGGILI
TPLPGATKLK PGSATQPFFG VVPEIVDADG KVLEGETTGN LCLTRAWPGM MRTVYGDHAR
FEQTYFSTYK GKYFTGDGCR RDADGYYWIT GRVDDVINVS GHRMGTAEVE SALVAHEKVS
EAAVVGFPHD IKGQGIYAYV TLMAGVQPTE DLRKELVTWV RKEIGPIASP DQIQFAPGLP
KTRSGKIMRR ILRKIAEDEP GSLGDTSTLA DPAVVDDLVK NRQNKKSA
//
