ACSA_METTP
ID ACSA_METTP Reviewed; 659 AA.
AC A0B8F1;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
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;
GN Name=acsA; Synonyms=acs; OrderedLocusNames=Mthe_1194;
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RX PubMed=22927778; DOI=10.1155/2012/315153;
RA Berger S., Welte C., Deppenmeier U.;
RT "Acetate activation in Methanosaeta thermophila: characterization of the
RT key enzymes pyrophosphatase and acetyl-CoA synthetase.";
RL Archaea 2012:315153-315153(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:0000269|PubMed:22927778}.
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 Evidence={ECO:0000269|PubMed:22927778};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CP000477; ABK14975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0B8F1; -.
DR SMR; A0B8F1; -.
DR STRING; 349307.Mthe_1194; -.
DR EnsemblBacteria; ABK14975; ABK14975; Mthe_1194.
DR KEGG; mtp:Mthe_1194; -.
DR HOGENOM; CLU_000022_3_6_2; -.
DR OMA; DHWWHDL; -.
DR BRENDA; 6.2.1.1; 11925.
DR SABIO-RK; A0B8F1; -.
DR Proteomes; UP000000674; Chromosome.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
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 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 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..659
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000429050"
FT BINDING 206..209
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 400..402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 424..429
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 600
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
SQ SEQUENCE 659 AA; 74109 MW; E714A49C59FB871A CRC64;
MAETAKTAVL QEETRIFNTP QWIIEYSNSY QWMKKKGFKT EKEMREWCAQ NYLDFWDEMA
QTYADWFKPY TQILEWNPPY AKWFLGGKCN VAHNAVDRHA KSWRRNKVAY YFVGEPVGDT
KTITYYQLYQ AVNKMANGLK SLGVKKGDRV SIYLPMIPEL PITMLACAKI GAIHSVVFSG
FSAGGLQSRV TDAEAKVVVT SDGFYRRGKP LPLKPNVDEA VQNAPSVEKV VVVKRVGLDV
PMKEGRDIWY HDLVKDQPAE CYTEELDPED RLFILYTSGT TGKPKGIEHA HGGFCVGPAY
TTAWALDVHE EDVYWCTADC GWITGHSYVV YGPLCLGATS ILYEGAPDYP DIGRWWSIIE
EYGVSVFYTA PTAIRMFMKA GDQWPKKYNL KSIRILASVG EPLNPEAYVW FRNNIGGGQA
PIIDTWWQTE TGCHVIAPLP MTPEKPGSVA FPLPGFNTDI YDEDGNSVPL GYGGNIVQKT
PWPSMLRAFF RDPERYMKEY WQMYWDIKPG TYLAGDKATR DKDGYWWIQG RIDDVLKVAG
HRISNAEVES AAVSHPAVAE AAVIGKPDEV KGEVIVAFII LKEGVQESED LKKDIAKHVR
SVLGPVAYPE IVYFVKDVPK TRSGKIMRRV IKAKALGKPV GDISALANPE SVENIPLIV
