ID   V4LUZ8_9CREN            Unreviewed;       715 AA.
AC   V4LUZ8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:ESQ22871.1};
GN   ORFNames=MGAcid_06900 {ECO:0000313|EMBL:ESQ22871.1};
OS   uncultured Acidilobus sp. MG.
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus; environmental samples.
OX   NCBI_TaxID=1410573 {ECO:0000313|EMBL:ESQ22871.1, ECO:0000313|Proteomes:UP000017902};
RN   [1] {ECO:0000313|EMBL:ESQ22871.1, ECO:0000313|Proteomes:UP000017902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT   "Predominant Acidilobus-like populations from geothermal environments of
RT   Yellowstone National Park exhibit similar metabolic potential in different
RT   hypoxic microbial communities.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESQ22871.1}.
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DR   EMBL; AYMA01000002; ESQ22871.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4LUZ8; -.
DR   STRING; 1410573.MGAcid_06900; -.
DR   PATRIC; fig|1410573.3.peg.647; -.
DR   Proteomes; UP000017902; 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: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; 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.
PE   4: Predicted;
FT   DOMAIN          9..103
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   715 AA;  75854 MW;  E0189DFA32FED4B3 CRC64;
     MYTAGAEVFF EPKKVAVVGA SPRPDNLGRA ILENLLTGFK GKVYVVNPGY TEVLGLKSYP
     SVQAVPDEVD LVVVATPARL APRVVEDAGA KGAKGVVVFS GGFAETGTDE GRRLQEEVVE
     VAKRHGVRLL GPNCIGVYNY SNGLDTFFLP RSKMKRPPPG PIAVVSQSGA LLATLMDWAA
     ARNIGIGKAI NFGNKADVDE VDSLEYMAKA PDVKAMVVYL EGVTRGRALI DAIRLNVNEG
     KPVIVVKGGR SQATARATLS HTASIAGSYD VFKEAMREAG ALLFEDLEAA FDAAKVLVSQ
     PLPRGPRVGI ITNSGGHGVI AADTVTAEGL EVPETPAAIA SSLRQIFPDR VSLRNPIDLT
     GDARPEQYKL VAQALVKGGL VDSLLLISLV QPPTMDVDET LRTIELIRDD SEGVPLVVVT
     IGAEAGAKLA RALEELGIPT FELPDRAARA LASLLHFRRA KDIIKPRGPA PTVSKEAFAR
     AKEIIQRALS QGRSKLLEDE ALELLRAYGV KVADFCVARS EEEASACAER VGPRLAMKVI
     SPDISHKSDV GGVLVGVTPE TAVSSYRAII NNVKSRAPGA RVEGVLVQRL ESGHEVMVGG
     LNDIAFGPVV TFGAGGLLVE LLGDVAMRLS PLDQEEALEM IKATKVYRLL KGFRGETPAN
     IDAIADIVVK VSLLLNDHNE IKELDINPIL ANQETATAVD ARVIVARGGG QPVVQ
//