ACSA_AGRRH
ID ACSA_AGRRH Reviewed; 652 AA.
AC Q9KWA3;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
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}; ORFNames=riorf81;
OS Agrobacterium rhizogenes.
OG Plasmid pRi1724.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX NCBI_TaxID=359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MAFF03-01724;
RX PubMed=10907845; DOI=10.1093/dnares/7.3.157;
RA Moriguchi K., Maeda Y., Satou M., Kataoka M., Tanaka N., Yoshida K.;
RT "Analysis of unique variable region of a plant root inducing plasmid,
RT pRi1724, by the construction of its physical map and library.";
RL DNA Res. 7:157-163(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MAFF03-01724;
RX PubMed=11273700; DOI=10.1006/jmbi.2001.4488;
RA Moriguchi K., Maeda Y., Satou M., Hardayani N.S.N., Kataoka M., Tanaka N.,
RA Yoshida K.;
RT "The complete nucleotide sequence of a plant root-inducing (Ri) plasmid
RT indicates its chimeric structure and evolutionary relationship between
RT tumor-inducing (Ti) and symbiotic (Sym) plasmids in Rhizobiaceae.";
RL J. Mol. Biol. 307:771-784(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}.
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DR EMBL; AB039932; BAA97792.1; -; Genomic_DNA.
DR EMBL; AP002086; BAB16200.1; -; Genomic_DNA.
DR RefSeq; NP_066662.1; NC_002575.1.
DR RefSeq; WP_010900271.1; NC_002575.1.
DR AlphaFoldDB; Q9KWA3; -.
DR SMR; Q9KWA3; -.
DR STRING; 359.CN09_18620; -.
DR eggNOG; COG0365; Bacteria.
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 Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Plasmid.
FT CHAIN 1..652
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208351"
FT BINDING 189..192
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 311
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 387..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 411..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 523
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 537
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 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
FT BINDING 584
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT MOD_RES 609
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123"
SQ SEQUENCE 652 AA; 71992 MW; 5B97DF7EAB99A8FB CRC64;
MSEKIYPVAK PVESHALINK AEYQEWYAES VADPEQFWGK HGKRIDWFKP YTSVKDTSFT
GDVSIKWFED GETNVSYNCI DRHLATNGDQ VAIIWEGDDP SLDRKITYRE LYEHVCRMAN
VLKKHGVKKG DRVTIYMPMV PEAAYAMLAC ARIGAIHSVV FGGFSPEALG GRIVDCQSTF
VITCDEGLRG GKPVPLKANV DKAIDIAARG HVMVKNVLVI RRTGSPLSWA PGRDLWHHEE
AATVSADCPP EPMKAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASMTHE YVFDYQHGDI
YWCTADVGWV TGHSYIVYGP LANCATTLMF EGIPTFPDAG RFWDVIDKHK VNIFYTAPTA
IRSLMGAGDD FVKRSSRSSL RLLGSVGEPI NPEAWEWYYH TVGDGRCPVV DTWWQTETGG
IMITPLPGAT DLKPGSATRP FFGIRPELVD AEGKLIEGAA DGNLCIADSW PGQARSVYGD
HERFIQTYFS TYEGKYFTGD GCRRDADGYY WITGRVDDVL NVSGHRLGTA EVESALVSHH
LVSEAAVVGY PHNIKGQGIY CYVTLMAGSE GSEELRQQLV KHVRAEIGPI ASPDKIQFAP
GLPKTRSGKI MRRILRKIAE DDFGSLGDTS TLADPAVVDD LIANRQNRAE AA
