ID K0NGA7_DESTT Unreviewed; 649 AA.
AC K0NGA7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=AcsA2: acetoacetyl-CoA synthetase {ECO:0000313|EMBL:CCK78843.1};
DE EC=6.2.1.1 {ECO:0000313|EMBL:CCK78843.1};
GN Name=acsA2 {ECO:0000313|EMBL:CCK78843.1};
GN OrderedLocusNames=TOL2_C06740 {ECO:0000313|EMBL:CCK78843.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK78843.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK78843.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
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DR EMBL; FO203503; CCK78843.1; -; Genomic_DNA.
DR RefSeq; WP_014956195.1; NC_018645.1.
DR AlphaFoldDB; K0NGA7; -.
DR STRING; 651182.TOL2_C06740; -.
DR KEGG; dto:TOL2_C06740; -.
DR PATRIC; fig|651182.5.peg.813; -.
DR HOGENOM; CLU_000022_3_3_7; -.
DR OrthoDB; 9801302at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd05943; AACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR005914; Acac_CoA_synth.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR01217; ac_ac_CoA_syn; 1.
DR PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCK78843.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT DOMAIN 36..92
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 96..426
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 649 AA; 72666 MW; 496358E61FE1AE1D CRC64;
MSKLLWQPSE ERIKSTNMYR FMKLVNEKFN TNLTDYPSLW EWSVDNLEDF WSTTWDFIDI
KASRLYEKAI DDPTKMPGAN FFVNSKLNFA ENLLRFRNDN IALIFKGENS VQRTLTYNQL
YDEVAKTAAS LKALGIQKGD RVVGFIPNMP ESIIAMLAAT SLGAIWSSCS PDFGIKGVLD
RFGQTRPKVL FTADGYFFKG KPLDSIKKIA GIVKEIPSIE KIVVIPYVSK EADIDSLPNS
VLFKDFKDPD ETEIQFEQMN FDDPLYVMYS SGTTGLPKCM VQSVGGVLLH QKKELVLHTD
LKEDDTIFYF TTCGWMMWNW LTCSLSVGAT LVLYDGNPFY PGPDALWKMA QDEKITIFGT
SAGYIEALKN TGVKPGKQFD LSALKSVLST GSPLSDENFE FIYNEVKKDI QLASIAGGSD
LNGCFFLGNP MGPVYTGELQ CKGLGMKVYA YDETGTPVVG QQAELVCTAP FPSMPVFFWG
DEDGSKYHSA YFDAYPGIWT HGDFIMITEN GGVIMLGRSD ATLNPGGVRI GTAEIYRRLD
AMEELEDSVI VGQSWDNDVR VILFVKLAKG FDLTNDLQNK IRTDIRANAS PRHVPAKIIE
CPDIPYTLNM KKVELAVKKM IEGKEVKNKD ALKNPDALDF FADIEELKS
//
