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
//