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
//