ID M1XL85_NATM8 Unreviewed; 672 AA.
AC M1XL85;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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:CCQ37267.1};
GN OrderedLocusNames=Nmlp_3127 {ECO:0000313|EMBL:CCQ37267.1};
OS Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS 8.8.11).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ37267.1, ECO:0000313|Proteomes:UP000011867};
RN [1] {ECO:0000313|EMBL:CCQ37267.1, ECO:0000313|Proteomes:UP000011867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC {ECO:0000313|Proteomes:UP000011867};
RX PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA Gross K., Schuster S.C., Oesterhelt D.;
RT "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT of a previously haloalkaliphilic genus.";
RL Genome Announc. 1:e0009513-e0009513(2013).
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DR EMBL; HF582854; CCQ37267.1; -; Genomic_DNA.
DR RefSeq; WP_015410014.1; NC_020388.1.
DR AlphaFoldDB; M1XL85; -.
DR STRING; 268739.Nmlp_3127; -.
DR GeneID; 14651715; -.
DR KEGG; nmo:Nmlp_3127; -.
DR eggNOG; arCOG01529; Archaea.
DR HOGENOM; CLU_000022_3_6_2; -.
DR OrthoDB; 371752at2157; -.
DR Proteomes; UP000011867; 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:CCQ37267.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011867}.
FT DOMAIN 56..101
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 114..497
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 560..638
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 652..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 74467 MW; 60EAC1BC113B3242 CRC64;
MTKDTEALRD EVVHDPSEAF VESTNVAAFM REYDIDDYDE LIERTTTDTG VDASGLEWFW
GELPEYLGIE FYQGYDAVRD DADGPQFTTW YPGAELNVAH NTVDRHGAPD AEARNSVACI
WEGEDGEVRE LTYHELRRRS NQVANYLESV GIDTGDTVGL YMPMVPEVIP ILYGCFKAGA
IAVPIFSGFG VDATAIRIED SRCSVLFTGD GFYRRGSEIT LKDAADDAIE EAGHVEHTVV
FDRLGASDDD AEIEIPFDGD RDEWFHDAVG TQDDDYGTKS LPADQECMLL YSSGTTGKPK
GIVHTHAGAQ LQPAKELHFG FDLKPADRFF WVSDIGWMMG PWTLVGTHTF GGTMVMYEGA
PDHPQPDRFW ELIDRHGVTQ FGISPTAIRA LRKHGDEWVE GYDLSSLRLL GSTGEPWDPE
SWLWFYEHVG GGDTPIINIS GGTEIFGCFL MPMPTRPLKP CTLGGPGLGM DIDIVDGTGE
SIREAHERGY LVARDSNPAM TKSLWGGDDR YLHEYWSTFE DPPMWNHGDW AQKDTEGFWF
LHGRADDALN VAGRKVGPAE VEGAAMEHDD VNQAAAVGVP DETTGTAVVL YVIVEEGAEE
TEASREAIRE LVGEEQGKPF RPREVLFVDE FPKTQSGKII RRAVEAAYTG EALGDMSSIE
NPDSLEELEE PR
//