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Database: UniProt
Entry: A0A1I0N0J0_9EURY
LinkDB: A0A1I0N0J0_9EURY
Original site: A0A1I0N0J0_9EURY 
ID   A0A1I0N0J0_9EURY        Unreviewed;       705 AA.
AC   A0A1I0N0J0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE            EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN   ORFNames=SAMN05216285_1210 {ECO:0000313|EMBL:SEV94544.1};
OS   Natrinema salifodinae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1202768 {ECO:0000313|EMBL:SEV94544.1, ECO:0000313|Proteomes:UP000183275};
RN   [1] {ECO:0000313|Proteomes:UP000183275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12284 {ECO:0000313|Proteomes:UP000183275};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOIS01000002; SEV94544.1; -; Genomic_DNA.
DR   RefSeq; WP_049990600.1; NZ_JROF01000017.1.
DR   AlphaFoldDB; A0A1I0N0J0; -.
DR   STRING; 1202768.SAMN05216285_1210; -.
DR   eggNOG; arCOG01340; Archaea.
DR   OrthoDB; 18103at2157; -.
DR   Proteomes; UP000183275; 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   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000183275};
KW   Transferase {ECO:0000313|EMBL:SEV94544.1}.
FT   DOMAIN          487..523
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   705 AA;  75232 MW;  6496934F89A5C927 CRC64;
     MGRLAELFDP ETVAVVGATD REGAVGRAIV ENLQDEFAGE IVPINPSRDE VLGLECYSDA
     KSAPPIDLAV VVVPPGVVID SVRELAETGT EHVVVITAGF AETGGEGAER ERRLREIAAE
     YDLDVVGPNS LGVMSTPNGM NATFGPESAL EGSISFMSQS GAFITAVLDW ANDQGIGFQD
     VVSLGNKTVV DETDFVREWG DDPDTDVIIG YLEDIDDGQA FLETAREVTG DTPIVLVKSG
     RTDAGAQAAS SHTGAIAGSE RAYEAGLEQA GVLRAQSVQE LFDYARALAG LPEPESDGVA
     VVTNAGGPGV LTTDAVGDST LEMADFADET IDELAEAMPD EANVYNPIDA IGDADVERFG
     EALEIALADP NVGSAVVVAA PTAVLSYDDL AETVIKKLET HDTPVVTCLM GGERARQAEE
     TLRESGIPNY FDPSRAVSGL DALARYRDIR ERTVDEPETF DVDRERAREI LQRAARRDDN
     RLGVESMDLL EAYGVPTPDG EIVDDPDRAR EVAESIEGDV VMKIVSPDIT HKSDIGGVKV
     GVSDDDVYDA YEDVVSRARN YQPDATIIGV QIQEMLDLDA GTETIVGMNR DPQFGPLLLF
     GLGGIFVEIL EDTSVRVAPI GEDEVRDMID EIRAAPLLRG ARGREPADVD AVVETVQRLS
     QLVTDFPSIL ELDVNPLVAG PDGAQAIDLR LTVDTDELDT ETDTE
//
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