ID K0JTS3_SACES Unreviewed; 661 AA.
AC K0JTS3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ECO:0000313|EMBL:CCH27638.1};
GN OrderedLocusNames=BN6_03060 {ECO:0000313|EMBL:CCH27638.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH27638.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH27638.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(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; HE804045; CCH27638.1; -; Genomic_DNA.
DR RefSeq; WP_015097752.1; NC_019673.1.
DR AlphaFoldDB; K0JTS3; -.
DR STRING; 1179773.BN6_03060; -.
DR KEGG; sesp:BN6_03060; -.
DR PATRIC; fig|1179773.3.peg.311; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_6_11; -.
DR OMA; DHWWHDL; -.
DR OrthoDB; 9803968at2; -.
DR BioCyc; SESP1179773:BN6_RS01500-MONOMER; -.
DR Proteomes; UP000006281; 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:UP000006281}.
FT DOMAIN 35..88
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 95..484
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 539..620
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT BINDING 198..201
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 317
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 341
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 393..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 417..422
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 MOD_RES 620
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ SEQUENCE 661 AA; 72263 MW; DDFFCE14673FAA21 CRC64;
MTQPQAQGPA LDNLLTENRT FPPSAEFAAQ ANATQELYDR AAADRDAFWA EQAERLVWDT
RWTQVLDWSN APFAKWFVGG RLNVAYNCVD RHVESGHGDQ VAIHWEGEPG DSRAITYAEL
QREVSKTANA LVELGVGAQD RVAIYMPMVP EAIFSMLACA RLGALHSVVF GGFSAEALRT
RIEDSQAKLV ITTDGQYRRG NPAALKPAVD EAVAKAASVE HVLVVKRTDS EVEWTEGRDL
WWHDLVDRQS DQHTPESFDS EHPLFILYTS GTTGNPKGIL HTSGGYLTQA SYTHHAVFDL
KPDTDVYWCT ADIGWVTGHS YIVYGPLSNR VTQVVYEGTP NTPHEGRHWE IVQKYGVSIY
YTAPTLIRTF MKWGADIPAK YDLSSLRVLG SVGEPINPEA WIWYRETVGA GKTPVVDTWW
QTETGAIMIS PLPGATSTKP GSAQRPLPGI GAKVVDDQGV EVGPGGGGYL VLDQPWPSML
RGIWGDEARY RDTYWSRFGE QGYYFAGDGA KYDDDGDIWL LGRVDDVMNV SGHRISTTEV
ESALVSHPTV AEAAVVGATD PTTGQGIVAF VILRGGVAEG SDGAAAIKAL REHVAKEIGP
IAKPRQILVV PELPKTRSGK IMRRLLRDVA ENRQVGDVTT LADSSVMDLI STGLKSGSTE
D
//