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Database: UniProt
Entry: A0A0S8FJT5_9GAMM
LinkDB: A0A0S8FJT5_9GAMM
Original site: A0A0S8FJT5_9GAMM 
ID   A0A0S8FJT5_9GAMM        Unreviewed;       898 AA.
AC   A0A0S8FJT5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:KPK60967.1};
GN   ORFNames=AMJ59_03060 {ECO:0000313|EMBL:KPK60967.1};
OS   Gammaproteobacteria bacterium SG8_31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK60967.1, ECO:0000313|Proteomes:UP000051321};
RN   [1] {ECO:0000313|EMBL:KPK60967.1, ECO:0000313|Proteomes:UP000051321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_31 {ECO:0000313|EMBL:KPK60967.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(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:KPK60967.1}.
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DR   EMBL; LJTI01000003; KPK60967.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8FJT5; -.
DR   PATRIC; fig|1703405.3.peg.595; -.
DR   Proteomes; UP000051321; Unassembled WGS sequence.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
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   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   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          502..538
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          743..897
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   898 AA;  98333 MW;  3F5FF528812C5F7E CRC64;
     MTLGTKGFGL DIGKLFEPRS IAVIGASERE GSPGAAVLRN LLSARFKGRV YPVNPKHEKV
     QRRRCYSSIR SIGKEIDLAV IVTPARAVPD VLEECGECGV DAAIVISAGF REIGEAGQAL
     ERSVVRVARR HGIRFLGPNC LGVMRPDIGL NATFSHCMAN KGRIALVSQS GALCTAILDW
     ARPRGIGFSC VISSGIAADV DFGEILDYLV LDARTGAIML YVEGLHDARR FMSALRAASR
     AKPVVVMKAG RHTQGGKAAA SHTGALVGSD EVFETAIRRA GVVRARRYDQ FFAAAATLHA
     GVRTAGPRLA IVTNGGGPGV IAADRLADVR LDLATLAKET RQRLDKHLPA AWSGNNPIDV
     LGDATPDRYA SALETCLSDP GVDAALAILV PQSISDPEAV AARVADISDR EAKPVFACWM
     GEKTMSSSRK LFLDRKVPTY STPEAAVDAF AAAAAYHTNQ QLLLQVPEPL SRQDHPSVDD
     ARMIIEAALS EKREMLDAVE SKAILAAFDI PILQSTPVRE MTEAIALAQE IGFPVAMKIR
     SHDITHKTDV DGVRLGLNSG HDIRKAWREM HEAVAKARPD ARIEGVMLER MWKPPAGREL
     MVGVLNDPVF GPVISVGLGG TMVEVIGDRS IALPPLNRYL VRRMIARTKA ARYLECFRGK
     PAASMEALED VILRVSEMVC ELPAVTEMDI NPLIVDERGA VAVDARIRVR HISTGAREYA
     HMAIHPYPST LVQELEMADG LRWTIRPIRP EDAVMEREFV NGLSDRSRYL RFMYVLNEIT
     PEMLSRFTQI DYDREMALIA VVHTEEGDHQ VGVARYVTYP DGRGCEFAIV VGDDWQRKGI
     ATRLLESLID VARDRRLETM DGIVLRENRN MLALAERVGF RQERSREDPE LMVLTLKL
//
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