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Database: UniProt
Entry: A0A2U0S338_9ARCH
LinkDB: A0A2U0S338_9ARCH
Original site: A0A2U0S338_9ARCH 
ID   A0A2U0S338_9ARCH        Unreviewed;       831 AA.
AC   A0A2U0S338;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:PVX25793.1};
DE   Flags: Fragment;
GN   ORFNames=CW691_03445 {ECO:0000313|EMBL:PVX25793.1};
OS   Candidatus Bathyarchaeota archaeon.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=2026714 {ECO:0000313|EMBL:PVX25793.1, ECO:0000313|Proteomes:UP000246112};
RN   [1] {ECO:0000313|EMBL:PVX25793.1, ECO:0000313|Proteomes:UP000246112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin-L-1 {ECO:0000313|EMBL:PVX25793.1};
RA   Yu T., Wu W., Liang W., Lever M., Hinrichs K.-U., Wang F.;
RT   "Growth of sedimentary Bathyarchaeota on lignin as an energy source.";
RL   Submitted (NOV-2017) 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:PVX25793.1}.
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DR   EMBL; PIXT01000073; PVX25793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U0S338; -.
DR   Proteomes; UP000246112; Unassembled WGS sequence.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
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; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR000182; GNAT_dom.
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; PF00583; Acetyltransf_1; 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   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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.
DR   PROSITE; PS51186; GNAT; 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:UP000246112}.
FT   DOMAIN          438..474
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          678..831
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PVX25793.1"
SQ   SEQUENCE   831 AA;  92680 MW;  458F11CFAC0D0F53 CRC64;
     QTVDQLPETV DLAVIATPAK TVPDMIEQCG KAGIVGVIII SAGFKEAGPE GKELEEKIVE
     TKRKYNIRIV GPNCLGVIRP SINLNATFTN KPPKQGNIAF ISQSGALGSA ILDWAIHENI
     GFSNFVSVGS MIDIDFGDLI DYFGTDPKTR SILMYIEGIT NARKFMSAAR HFARTKPIIV
     VKAGKFGETA KAVMSHTGAQ AGEDLAYAAA FKRVGIVRVE EIGDLFNCAE VLGVQPLPRG
     SKLAIITNAG GAGVMAADAL IAGGGKLAEL DPKTVEKLDK VLPPHWSKAN PIDILGDAKT
     GRYETAIMAC LGDKNVDGLL IVYAPQGVAD AVEIAESVSK LCEHKDFGKP ILTSFMGYEE
     VEEANRVLNE NSIPTYSTPE QAIKTYLYMN QYKRNLELLY QTPEELPVDS SPPKRPIEVV
     IRKTAKENRE NLTEIESKQI LENYKIPVIQ TLTAQTEDEA VFAASRIGYP LMLKILSPQI
     VHKTDNEVVC DIKSDAELKE SFRNVVQQAK KQNPDAQILG VTLQQMPKKL GYKIKLGART
     DSLFGPIVRF AMNNVNEAFD DVAVGLPPLN QALARRIMEE TQGYKLLKGY KNVPPANLKL
     LEEIMVRFSQ LLVDFPQIKE ADINPLFINH EEALALDAKI VIDKEQVSTK FEPHQHLVIS
     PYPKKYETSW KLRDGRNVLL RPIKPEDEPM WLEMFQNFSE QSIRYRFFQI IKDTPHEVRV
     RYSNIDYDRE IGIVAELKEE RRKILGVVRL IIEPDEKTGE IAFIVADPWQ GLGLGSKMVD
     YMIEICKDKH LETVYAFMLP DNHRAIRLLK KMGFTLKHTQ DVTKATLNLK E
//
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