ID K0DKF2_9BURK Unreviewed; 690 AA.
AC K0DKF2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=BUPH_01685 {ECO:0000313|EMBL:AFT85260.1};
OS Paraburkholderia phenoliruptrix BR3459a.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1229205 {ECO:0000313|EMBL:AFT85260.1, ECO:0000313|Proteomes:UP000010105};
RN [1] {ECO:0000313|EMBL:AFT85260.1, ECO:0000313|Proteomes:UP000010105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR3459a {ECO:0000313|EMBL:AFT85260.1,
RC ECO:0000313|Proteomes:UP000010105};
RX PubMed=23144415; DOI=10.1128/JB.01821-12;
RA de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G.,
RA Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I.,
RA Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M.,
RA Ribeiro de Vasconcelos A.T.;
RT "Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a
RT Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa.";
RL J. Bacteriol. 194:6675-6676(2012).
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}.
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DR EMBL; CP003863; AFT85260.1; -; Genomic_DNA.
DR AlphaFoldDB; K0DKF2; -.
DR STRING; 1229205.BUPH_01685; -.
DR KEGG; bpx:BUPH_01685; -.
DR PATRIC; fig|1229205.11.peg.1282; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_4; -.
DR Proteomes; UP000010105; Chromosome 1.
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}.
FT DOMAIN 62..116
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 124..510
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 574..655
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 227..230
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 347
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 427..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 451..456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 566
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 580
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 585
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT MOD_RES 655
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ SEQUENCE 690 AA; 75325 MW; 83D1E23FA23087E3 CRC64;
MNRKPIAALN MTWRTPCAPA QVFIFTKGLS MSAIESVLQE RRVFPPSAET AAGATISGMD
AYHALAAEAE RDYEGFWGRL ARETLSWNTP FTKVLDESNA PFYTWFEDGQ LNASYNSIDR
HVEAGNGGRV AIIFEADDGT VTNVTYQDLL QRVSRFANAL KKRGVKKGDR VVIYMPMSIE
GIVAMQACAR IGATHSVVFG GFSSKSLNER LVDVGAVALV TSDEQMRGGK ALPLKNIADE
ALAMGGCDAV KSVIVYKRTG GKIAWNEGRD LWMHELSQAE SDQCAPEWVG AEHPLFILYT
SGSTGKPKGV QHSTGGYLLW AAQTMKWTFD WKPSDVFWCT ADIGWITGHS YITYGPLTLG
GTQVVFEGVP TYPNAGRFWD MIAKHKVSLF YTAPTAIRSL IKASEADQKV HPKSYDLSTL
RIIGTVGEPI NPEAWVWYHE NVGGGRCPIV DTWWQTETGG HMITPLPGAT PLVPGSCTLP
LPGIMAAVVD ETGQDVPNGQ GGILVVKRPW PSMLRNVWGD PDRYKKSYFP EELGGKLYLA
GDGAVRDKET GYFTIMGRID DVLNVSGHRL GTMEIESALV SNPIVAEAAV VGRPDATTGE
AVCAFVVLKR ARPEGEEAVK LANELRNWVG KEIGPIAKPK DIRFGENLPK TRSGKIMRRL
LRSLAKGEAI TQDVSTLENP AILDQLGESL
//
