ID A0A0S8C8E0_9PROT Unreviewed; 901 AA.
AC A0A0S8C8E0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:KPK19308.1};
GN ORFNames=AMJ67_05590 {ECO:0000313|EMBL:KPK19308.1};
OS Betaproteobacteria bacterium SG8_41.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK19308.1, ECO:0000313|Proteomes:UP000051544};
RN [1] {ECO:0000313|EMBL:KPK19308.1, ECO:0000313|Proteomes:UP000051544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_41 {ECO:0000313|EMBL:KPK19308.1};
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:KPK19308.1}.
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DR EMBL; LJTT01000014; KPK19308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8C8E0; -.
DR STRING; 1703391.AMJ67_05590; -.
DR PATRIC; fig|1703391.3.peg.2371; -.
DR Proteomes; UP000051544; 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 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 501..537
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 742..899
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 901 AA; 96357 MW; 5F30F97462B29489 CRC64;
MSTLHTARHY FAPLFEPGAV AIIGASERPG SVGAVLMQNM LGAGYLGKLY GVNPKRRSVQ
GMPCFATIGE VPRRVDLAVI ATPAATVPEI INACGEAGVR ATVVISAGFS ESGPAGAKLE
RALLENARRH RLRVLGPNCL GILRPDIGLN ASFARGRALP GSLGLISQSG AVCTAMLDWA
TPNGVGFSCI ASLGASTDVD FGEIVDYLVN DPVTEHILLY IEGVRDARRF MSALRAAARV
KPVILMKVGR QPAGSRAAMS HTGALVGADD VFDAAVRRAG VVRVGTIGEL VAAAHALSAH
VRARGDRLAV ITNGGGPGVM AADRAADLGI PLSRLAPATI EVLVKALPPN WSQGNPVDLI
GDADAARYRA ALLACLADRG VDGVLVILTP QAMTEPLEVA KVVVECARSS DKPLLACWMG
EGQVAEGWRL LAERRIPVFR TPDPAVAMFA HVSAFYRNQK MLLQTPGPLS DYPAPDVAGA
RLVIETALGE RRTVVSEMES KAVLAAFRVP IARAVRVHSP DEAMLIAQEF GFPVAMKIDS
PDVTHKSDVG GVKLNIANGQ AAREAYREIS EGVARLRPGA RVSGIIVEPM VLRPNSRELM
VGVVCDPVFG PAITFGTGGT AVEIHADRAV ALPPLDAVLV DELIRGTRAS RVLGEFRHMP
PVDRTALEAV LLRVSEMVCE LPWIREMDIN PLLLDESGAV ALDARIVVGR PAPALRRYGH
MAIHPYPSRL VSEWSAPDGR RVTVRPIRPE DAQVEQEFVK QLSAEARYFR FMDTIRELTP
QMLVRFTQID YDREMAFVAI VSGPDGRDTE VAVARYITNP DGLSCEFAIV VDDEWQRAGL
GRYLMTQLIE VARARELASM SGEILAANTG MLKLAASMGF RIGESPADPS LRRATLNLAP
S
//
