ACSA_MYCS2
ID ACSA_MYCS2 Reviewed; 940 AA.
AC A0R5G1; I7GA85;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Acetyl-coenzyme A synthetase;
DE Short=AcCoA synthetase;
DE Short=Acs;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase;
DE AltName: Full=Acyl-activating enzyme;
DE Flags: Precursor;
GN Name=acsA; OrderedLocusNames=MSMEG_6179, MSMEI_6020;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION.
RX PubMed=21627103; DOI=10.1021/bi200156t;
RA Xu H., Hegde S.S., Blanchard J.S.;
RT "Reversible acetylation and inactivation of Mycobacterium tuberculosis
RT acetyl-CoA synthetase is dependent on cAMP.";
RL Biochemistry 50:5883-5892(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:0000269|PubMed:21627103}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PTM: Acetylated on Lys-906 by Pat in the presence of acetyl-CoA as an
CC acetyl donor and ATP. Acetylation results in the inactivation of the
CC enzyme. Deacetylation by the SIR2-homolog deacetylase CobB is required
CC to activate the enzyme (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP42452.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK69538.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42452.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_890399.1; NC_008596.1.
DR AlphaFoldDB; A0R5G1; -.
DR SMR; A0R5G1; -.
DR STRING; 246196.MSMEI_6020; -.
DR EnsemblBacteria; ABK69538; ABK69538; MSMEG_6179.
DR EnsemblBacteria; AFP42452; AFP42452; MSMEI_6020.
DR KEGG; msg:MSMEI_6020; -.
DR KEGG; msm:MSMEG_6179; -.
DR PATRIC; fig|246196.19.peg.6019; -.
DR eggNOG; COG0365; Bacteria.
DR OMA; DHWWHDL; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 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; Reference proteome; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..940
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000420242"
FT REGION 1..289
FT /note="Unknown"
FT REGION 70..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..940
FT /note="Acetyl-coenzyme A synthetase"
FT COMPBIAS 70..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..483
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 675..677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 699..704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 796
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 811
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 819
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 822
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 833
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 835
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 838
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 906
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 940 AA; 99957 MW; 18AB5298FB108F45 CRC64;
MCCAIWSASR APACSASQLS SSHAVRPSVV PDANPRAAPR YSPDLRIQCT SGTPRPCGSS
PLAIVTSRET ARATTPSAVP NGASVSNSPC ATAASTGAGA LDPPVRSSIS NSRRGPTSGS
VRGRPRCSSS VRSAAASACS RASACIGARC HTVTNEVAPP SSASATRIAP AVTGSGSPSA
DSCTAPPSST ADARAPRSAD SAAVCGQPRR LTLCRCARPS ASRASSQAAA TPGSSNSGAR
GSGRSVITSH ASRPLIASSP TVQRNQTTVH QQTCEGPTCV QRSVTRLTAM SNPSHAEVPS
AYPPPADFAA NANATGELYA EAEKDRLAFW EKQAKRLSWQ TPFTDVLDWS DAPFAKWFVG
GKINVAYNCV DRHVEAGNGD RVAIHWEGEP VGDARSITYA ELKDEVCKAA NALTDLGLVA
GDRVAIYMPM IPEAIVAMLA CARLGVMHSV VFAGFSASAL RARIEDAEAK LVITSDGQYR
RGKAASLKEA VDEAVADQPS VKNVLVVRRT GIDVKWTDGR DLWWDETVEQ ASTEHIPAAF
DSEQPLFLLY TSGTTGKPKG IVHTSGGYLT QSSYTHWNVF DVKPESDVYW CTADIGWVTG
HTYIVYGPLS NGVTQVVYEG TPTSPTEHRH FEVIEKYGVT IYYTAPTLIR TFMKLGHQIP
ASHDLSSLRL LGSVGEPINP EAWRWYREHI GGGKTPIVDT WWQTETGAIM ISPLPGVTAA
KPGSAMTPLP GISAKIVDDE GNQLVPGADE AEHVTGYLVL DQPWPAMLRG IWGDPQRFKD
TYWSRFAEQG WYFAGDGARY DSDGHIWVLG RIDDVMNVSG HRISTAEVES ALVGHAGVAE
AAVVGASDDT TGQAICAFVI LKASAHGGPE NMIEELRAEV AREISPIAKP REIHIVPELP
KTRSGKIMRR LLRDVAEGRE LGDTSTLVDP SVFEAIRASK
