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Database: UniProt
Entry: A0A0P9DNB8_9ARCH
LinkDB: A0A0P9DNB8_9ARCH
Original site: A0A0P9DNB8_9ARCH 
ID   A0A0P9DNB8_9ARCH        Unreviewed;       403 AA.
AC   A0A0P9DNB8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:KPV61615.1};
GN   ORFNames=AOA65_2213 {ECO:0000313|EMBL:KPV61615.1};
OS   Candidatus Bathyarchaeota archaeon BA1.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1700835 {ECO:0000313|EMBL:KPV61615.1, ECO:0000313|Proteomes:UP000050312};
RN   [1] {ECO:0000313|EMBL:KPV61615.1, ECO:0000313|Proteomes:UP000050312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA1 {ECO:0000313|EMBL:KPV61615.1};
RX   PubMed=26494757; DOI=10.1126/science.aac7745;
RA   Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA   Golding S.D., Tyson G.W.;
RT   "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT   genome-centric metagenomics.";
RL   Science 350:434-438(2015).
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:KPV61615.1}.
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DR   EMBL; LIHJ01000088; KPV61615.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P9DNB8; -.
DR   STRING; 1700835.AOA65_2213; -.
DR   KEGG; barc:AOA65_2213; -.
DR   PATRIC; fig|1700835.3.peg.2705; -.
DR   Proteomes; UP000050312; Unassembled WGS sequence.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
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; 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; PF13380; CoA_binding_2; 1.
DR   Pfam; PF19045; Ligase_CoA_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE   4: Predicted;
FT   DOMAIN          5..75
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF13380"
FT   DOMAIN          92..230
FT                   /note="Succinyl-CoA synthetase-like flavodoxin"
FT                   /evidence="ECO:0000259|Pfam:PF13607"
FT   DOMAIN          243..391
FT                   /note="Ligase-CoA"
FT                   /evidence="ECO:0000259|Pfam:PF19045"
SQ   SEQUENCE   403 AA;  43820 MW;  79DF0972A12A917E CRC64;
     MDLIPDEVDT AIIATPASTV VEIMESCARK GVKAAIVVSS GFSEEGNKRL EQEIVKIAKR
     AGIRVIGPNT TGVLNTANNF ITTFVPIENL RRGNVALVAQ TGMFLGAMLR SIASSQHFGV
     SKVVGLGNKC DVDDWEALEY LAQDPETALI GMYIEGIKDG RGFLEVSQRV TKEKPVLILK
     SGITEVGSKV VLSHTGSLSG KDEVFDAACK QAGIIRVRSL EELIDLTKAF AFQPLPRGNR
     VAVVSFTGAG GVIATDACAE NGLAVARISR ETEKRLRRVT PKWHRILNPV DLWPAVEASG
     TIEACNTAIK AIVEDEGVDE VIVILAVFKG MVLPCDLDIL KEKRHLDKPL LFCIIGDKDY
     AELMTGVLER RGFPVYPYIT RAVKASAAMH RYSAQRKRLC LLF
//
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