ID E0TCV3_PARBH Unreviewed; 659 AA.
AC E0TCV3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=PB2503_09194 {ECO:0000313|EMBL:ADM09892.1};
OS Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 / KCTC 12087).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Parvularcula.
OX NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM09892.1, ECO:0000313|Proteomes:UP000001302};
RN [1] {ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RA Kang D.-M., Oh H.-M., Cho J.-C.;
RT "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADM09892.1, ECO:0000313|Proteomes:UP000001302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC {ECO:0000313|Proteomes:UP000001302};
RX PubMed=21037002; DOI=10.1128/JB.01205-10;
RA Oh H.M., Kang I., Vergin K.L., Kang D., Rhee K.H., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2503T of Parvularcula bermudensis,
RT the type species of the order "Parvularculales" in the class
RT Alphaproteobacteria.";
RL J. Bacteriol. 193:305-306(2011).
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; CP002156; ADM09892.1; -; Genomic_DNA.
DR RefSeq; WP_013300866.1; NC_014414.1.
DR AlphaFoldDB; E0TCV3; -.
DR STRING; 314260.PB2503_09194; -.
DR KEGG; pbr:PB2503_09194; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_5; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000001302; 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 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:UP000001302}.
FT DOMAIN 33..90
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 92..477
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 539..617
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 200..203
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 319
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 395..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 419..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 531
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 547
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 592
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT MOD_RES 617
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ SEQUENCE 659 AA; 72331 MW; 66596030DE97BADA CRC64;
MAHLAEQTVA PAERVHPVPA DFAQKTNLDP AGYLAMRQEA ETDPVAFWAR EGQRLDWIEP
YTKVKDTSFD LQDFRIKWYE DGVLNVAANC LDRHLKTRGD KPAIIWEADD PSKSRTLTYR
DLFEEVCRFA NVLKDLGVER GDRVTLYLPM IPEAAVAMLA CARIGAIHSV VFAGFSPEAL
AGRLIDCGSQ VIVTADGGVR GGKSVPLKAN VDRACEQEGV DVHSVLVIRR TDDPVKMVEG
RDHWLEDCAA LVSAECPAVP MGAEDPLFIL YTSGSTGKPK GVLHTSGGYL VWAAMTHEYA
FDLKEDDVYW CSADIGWVTG HSYIVYGPLA NGATTVMFEG VPTWPDASRF WQVVDKHQVS
TFYTAPTAIR ALMREGDAPV QATSRKSLRL LGTVGEPINP EAWEWYYRTV GEARCPIVDT
WWQTETGGTM MMPIPGTTDQ KPGAASHPFF GVTPALLDAE GRELTGAAEG NLVIRDSWPG
QMRTVYGDHQ RFIDTYFSAY PGNYFTGDGC RRDADGFYWI TGRVDDVLNV SGHRMGTAEI
ESALVAHPAV AEAAVVGYPH DLKGQGIYAY VTLKAGQEGD DDLRRGLIRH VRAEIGPIAI
LDKVQFAPGL PKTRSGKIMR RILRKIAENS IDSLGDTSTL ADPGVVDELI AHRCSDIVA
//
