ID   F2LIX9_BURGS            Unreviewed;       563 AA.
AC   F2LIX9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Acyl-coenzyme A synthetase {ECO:0000313|EMBL:AEA63356.1};
GN   OrderedLocusNames=bgla_2g08940 {ECO:0000313|EMBL:AEA63356.1};
OS   Burkholderia gladioli (strain BSR3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA63356.1, ECO:0000313|Proteomes:UP000008316};
RN   [1] {ECO:0000313|EMBL:AEA63356.1, ECO:0000313|Proteomes:UP000008316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSR3 {ECO:0000313|EMBL:AEA63356.1,
RC   ECO:0000313|Proteomes:UP000008316};
RX   PubMed=21478339; DOI=10.1128/JB.00420-11;
RA   Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA   Moon J.S., Kim J., Hwang I.;
RT   "Complete genome sequence of Burkholderia gladioli BSR3.";
RL   J. Bacteriol. 193:3149-3149(2011).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP002600; AEA63356.1; -; Genomic_DNA.
DR   RefSeq; WP_013689683.1; NC_015376.1.
DR   AlphaFoldDB; F2LIX9; -.
DR   STRING; 999541.bgla_2g08940; -.
DR   KEGG; bgd:bgla_2g08940; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_59_10_4; -.
DR   Proteomes; UP000008316; Chromosome 2.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
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   PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT   DOMAIN          50..387
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          453..530
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   563 AA;  63222 MW;  CCE906F2D6755A28 CRC64;
     MTAQAFLDAR DFLLRHRTDY DTAYRDFRWP QLASFNWALD YFDAMAHGNE RPALWIVDAA
     TGVGEPVSFA RMSEQSSRIA NHLRRLGVGR GDRLLLMLPN RVELWETMLA AMKLGAVVLP
     ATTQLPAEEI RDRVTIGGAR YAVIDAAEAA KFDQAGVEVT RIIVGGAREG WLRYDEGYAA
     PAEFAPDAPT HVDDTLLLYF TSGTTSKPKL VEHTHRTYPV GSLSTLYWIG LQPGDIHWNI
     SSPGWAKHAW SCFFAPWNAQ ACVFAFNYTR FDPKQALDAL VRYGITTLCA PPTVWRMLVQ
     QPLASYAVKL REIIGAGEPL NPEIIERVRR AWGITIRDGY GQTETTCLIG NSPGQPVVAG
     SMGRPLPGYR VALLDPDGAP VEEGEIALPL DGERPAGLMT GYDNHAEATA RAMRDGYYRT
     SDIALRRDDG YYLYIGRADD VFKSSDYRLS PFELESVLIE HPAIAEAAVV PSPDPLRLSV
     PKTVVMLRTG YEPDAALARE IFRFSREKLA PYKRIRRLQF AELPKTISGK IRRVELRRRE
     LERDADPSLR MPDEYWEEDF PNE
//