ID   B0R3G8_HALS3            Unreviewed;       656 AA.
AC   B0R3G8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE            EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN   Name=acs1 {ECO:0000313|EMBL:CAP13282.1};
GN   OrderedLocusNames=OE_1726F {ECO:0000313|EMBL:CAP13282.1};
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX   NCBI_TaxID=478009 {ECO:0000313|EMBL:CAP13282.1, ECO:0000313|Proteomes:UP000001321};
RN   [1] {ECO:0000313|EMBL:CAP13282.1, ECO:0000313|Proteomes:UP000001321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1 {ECO:0000313|Proteomes:UP000001321};
RX   PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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DR   EMBL; AM774415; CAP13282.1; -; Genomic_DNA.
DR   RefSeq; WP_010902316.1; NC_010364.1.
DR   AlphaFoldDB; B0R3G8; -.
DR   EnsemblBacteria; CAP13282; CAP13282; OE_1726F.
DR   GeneID; 68693392; -.
DR   KEGG; hsl:OE_1726F; -.
DR   HOGENOM; CLU_000022_3_6_2; -.
DR   PhylomeDB; B0R3G8; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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   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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAP13282.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          37..92
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          102..483
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          544..622
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   656 AA;  71511 MW;  8C5ED2298860DE3D CRC64;
     MDSLDGVGTV VHEPDPALAS STNVAQFMTA HDIDDVDALR ERSTTDLDWF WGELPEYLGL
     EFFEDYDAVR DDADDPQSTA WYPGAELNVA HNTVDRHASV DAGTRNHVAC IWEGEDGTVR
     QQTYHDLHQQ ANRVANALAE RGIGEGDTVG LYMPMVPEVQ SILYGIFKIG AIAVPIFSGF
     GVEATATRIA DAECSVVFTG DGFLRRGDRV TLMDTLNDAI ERAGHVDHTI VYDRLGIPAD
     SLSWTPRDEW WDDAVATQSP TFETHSMAAS DPCMLLYSSG TTGTPKGIVH THAGALVQPA
     KEIHFGFDQR PGDRFCWVSD IGWMMGPWSL IGNHAFAGTI VMYEGAPDHP APDRFWQLIE
     DHGITQFGVS PTAIRALRDH GDEHVAGHDL SSLRILGSTG EPWDPESWRW FYDHVGGGDT
     PIINISGGTE VFGCFLMPLP TESLKPCTLG GPGLGMDIDI VDDDGTSVRD ANERGYLVAR
     SSSPSMTRRL WSGEDRYLEA YWSRFEDVWN HGDWAQMDAD GDWFLHGRAD DAINVAGRKV
     GPAEVEGALI DHDAVTQAAV VGVPDDTTGE AAIAYVILAD AATPSAELRA ELRDHVGDAH
     GKPFRPREVV FVDDLPKTQS GKLVRRAVAS AYTGADVTDR SSIENPAVLD ALRDAT
//