ID   U1QN10_9EURY            Unreviewed;       697 AA.
AC   U1QN10;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE            EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN   ORFNames=J07HN4v3_02599 {ECO:0000313|EMBL:ERH06972.1};
OS   Halonotius sp. J07HN4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halonotius.
OX   NCBI_TaxID=1070774 {ECO:0000313|EMBL:ERH06972.1, ECO:0000313|Proteomes:UP000030639};
RN   [1] {ECO:0000313|EMBL:ERH06972.1, ECO:0000313|Proteomes:UP000030639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J07HN4 {ECO:0000313|Proteomes:UP000030639};
RX   PubMed=23637883;
RA   Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA   Allen E.E.;
RT   "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL   PLoS ONE 8:E61692-E61692(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate;
CC         Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456216; EC=6.2.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001619};
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DR   EMBL; KE356578; ERH06972.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1QN10; -.
DR   eggNOG; arCOG01340; Archaea.
DR   HOGENOM; CLU_007415_3_1_2; -.
DR   Proteomes; UP000030639; Unassembled WGS sequence.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR043938; Ligase_CoA_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF19045; Ligase_CoA_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030639}.
FT   DOMAIN          486..522
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   697 AA;  73911 MW;  A1756BACF977CF50 CRC64;
     MGTLTELFAP DRIAVVGATA REGSIGRAVT DNILSAFDGE VVPVNPNYEE VLGLSCVDAV
     GEAAADMAVI VVPPKIVLPA IEQAGEAGVE NVVVITAGFG ETGGDGASRE RELKEIAAEY
     DLNLVGPNSL GIMSTANGMN ASFGPDSPQA GNMSFMSQSG AFITAVLDWA NDEDVGFKDV
     ASLGNKAVLD ETDFVDHWGD DPDTDVIIGY LEGISQGREF IDTAREVTQE TPIVLVKSGR
     TDAGAQAASS HTGTIAGSEQ AYEAGLDQAG VLRAESVQGL FDAAQMLANQ PVPDNNDIAV
     ITNAGGPGVM STDAIGDSDL TMASFEQETL DTFSEQLPPE GNIYNPVDIV GDADVERFRD
     ALDTALADEN VGSAMVLSCP TAVLDYEQLA AETVELREKH GKPVAACFMG GESVDASAEI
     LKDAGIPNYF DPSRAIGALD ALWEYRGIQR RTYEEPANFD VDRDAAREIL ERVEDRTDNR
     LGVEAMGLLD AYGIPTPDSE IVDAPEDARA VAEEIEGDVV MKIVSPDILH KSDIGGVAVG
     IADDEVADTY ETLITRARNY QPDANLLGVQ VQEMADLDSG TETIVGMNRD PQFGPLMMFG
     LGGIFVEVLE DTTFRVAPVS KTEAREMTEE IKTAPLLRGA RGRDAADIDG IVETIQRLSQ
     LVADFPAIME FDINPLVATP DGVDAVDIRL TVDPENL
//