ID A0A0Q4KU35_9SPHN Unreviewed; 643 AA.
AC A0A0Q4KU35;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ASE86_05030 {ECO:0000313|EMBL:KQN25581.1};
OS Sphingomonas sp. Leaf33.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN25581.1, ECO:0000313|Proteomes:UP000051455};
RN [1] {ECO:0000313|EMBL:KQN25581.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN25581.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN25581.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN25581.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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: 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:KQN25581.1}.
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DR EMBL; LMLB01000001; KQN25581.1; -; Genomic_DNA.
DR RefSeq; WP_056423158.1; NZ_LMLB01000001.1.
DR AlphaFoldDB; A0A0Q4KU35; -.
DR STRING; 1736215.ASE86_05030; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000051455; 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:UP000051455}.
FT DOMAIN 22..79
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 81..465
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 527..605
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 331
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 496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 519
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT BINDING 580
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
FT MOD_RES 605
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01123"
SQ SEQUENCE 643 AA; 70364 MW; FC059E42CFF2016E CRC64;
MSDVYRVPED WARHAHVDAD RYAALYDAAA SDPDRFWLDQ AQRLDWIVPP TVADESSFDE
ADFGVRWFAD GRLNVAANCL DRHLASRGNA IALIWEPDAP EEEPKRFTYL ELFQHVCRFA
NVLKAEGVAK GDRVTIYMPM IPEAAFAVLA CARIGAIHSV VFGGFSPDAL AGRIVDCDSR
IVVTADCGRR GGKTIPLKAN VDAAAERAPS LERVIIVRAT GADVPMTPRD VWYHEAADTV
SADCPAEPMD AEDPLFILYT SGSTGKPKGV LHSSAGYLLW ASLTHHWCFD YRSGDVWWCA
ADIGWVTGHS YILYGPLANG ATTLMYEGLP NWPDASRIWQ VVDRHKVHTI FTAPTALRAL
MKDGDDFVGR TDRSSLKLLG TVGEPINPEA WRWYHDVVGE GRCPIVDTWW QTETGAAMIA
PLPGATDLKP GSATKPLPGV HPELVDETGQ VLDGAVSGNL CITRSWPGQM RTVWGDHARF
FQTYFTTYPG KYFTGDGCRR DADGYYWITG RVDDVINVSG HRMGTAEVES ALVLHAKVAE
AAVVGMPHDV KGQGIYAYVT LNAGVDSSDD LRAELRQWVR SEIGPIATPD AIQFAPGLPK
TRSGKIMRRI LRKIAEGDVS SLGDTSTLAD PAVVDDLVAN RVG
//
