ID   A0A160T6K2_9CHLR        Unreviewed;       916 AA.
AC   A0A160T6K2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetyl coenzyme A synthetase (ADP forming), alpha domain protein {ECO:0000313|EMBL:CUS05644.1};
DE            EC=6.2.1.13 {ECO:0000313|EMBL:CUS05644.1};
GN   ORFNames=CFX0092_B0110 {ECO:0000313|EMBL:CUS05644.1};
OS   Candidatus Promineifilum breve.
OC   Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC   Candidatus Promineifilaceae; Candidatus Promineifilum.
OX   NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS05644.1, ECO:0000313|Proteomes:UP000215027};
RN   [1] {ECO:0000313|EMBL:CUS05644.1, ECO:0000313|Proteomes:UP000215027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cfx-K {ECO:0000313|EMBL:CUS05644.1,
RC   ECO:0000313|Proteomes:UP000215027};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LN890656; CUS05644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A160T6K2; -.
DR   KEGG; pbf:CFX0092_B0110; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000215027; Chromosome ii.
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; PF13302; Acetyltransf_3; 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; 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   Ligase {ECO:0000313|EMBL:CUS05644.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215027}.
FT   DOMAIN          518..554
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          759..916
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   916 AA;  100273 MW;  E3EAF9703D7D7954 CRC64;
     MSDNITRSTA HNVLRMEKNP LEVMFKPRSV AVVGATERPG SVARTILWNL ISTSFGGTIF
     PVNPKYNSIL GIKAYPSIGD IPDPVDLAVI VTPAPSVPAI IEECVAAGCH AAIIISAGFK
     ETGPAGAALE QEILKIARRG NMRIIGPNCL GVMNPITGLN ATFASTMARP GSVGFISQSG
     ALLTAILDWS FAENVGFSAF VSIGSMLDVG WGDLIYYLGD DPNTKAIVMY MESIGDARSF
     LSAAREVALT KPIIVIKPGR TEEAAKAAAS HTGSLTGGDE VLAAAFRRSG VLRVDSISDL
     FNMAEVLSKQ PRPRGPRLSI VTNAGGPGVL ATDALITNGG QLAPISDEAM AAYNKLLPAP
     WSHNNPIDIL GDADAGRYAE SIKIAINDHD SDGTLVILTP QAMTNPTETA RALVDQFARP
     AGHVYGKPIL ASWMGGPEVS SGKDMLNKAN IPTFDYPDTA ARIFNYMWRY QRRLTALYQT
     PEMAQDFGET GFKHYLIKEM LEQIRATGRT ILTEYESKQV LEAYDIPTTP TRLAGSADEA
     AAIAAEIGFP VVVKLNSETI THKTDVGGVR LDLTNADEVR NAFLTMEKAV AEKYSPRDFL
     GVTVQPMLRL HDGYELILGS SPDPQFGPVV LFGTGGTLVE VFKDRALAIP PLNTTLARLT
     MTRTKIYEAL KGVRGRPPVD LAELDKIFVR FSQLVIEQRW IKEIDINPLF ASHEQLIALD
     GRVVLYEPEV TEDQLPRLAI RPYPTNYVKQ FNNKGGEAFV LRPIRPEDEP KMVQFHEKLS
     EQSVYLRYFR AFKLDQRVEH ERLTRICYVD YDRTIALVVE HTDPATAETA IVAVARLTRL
     PNPEEAEFAM LVRDDFQGRG VGTQLLQNLL DFGRDEGIKR VVAFMLPENR GMIEISEKLG
     FAMGREDEMV KAVKEL
//