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Database: UniProt
Entry: A0A260B7H5_9NOCA
LinkDB: A0A260B7H5_9NOCA
Original site: A0A260B7H5_9NOCA 
ID   A0A260B7H5_9NOCA        Unreviewed;       648 AA.
AC   A0A260B7H5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acetoacetate--CoA ligase {ECO:0000313|EMBL:OZC99288.1};
GN   ORFNames=CH275_22615 {ECO:0000313|EMBL:OZC99288.1};
OS   Rhodococcus sp. 06-235-1A.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=2022508 {ECO:0000313|EMBL:OZC99288.1, ECO:0000313|Proteomes:UP000215839};
RN   [1] {ECO:0000313|EMBL:OZC99288.1, ECO:0000313|Proteomes:UP000215839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=06-235-1A {ECO:0000313|EMBL:OZC99288.1,
RC   ECO:0000313|Proteomes:UP000215839};
RA   Savory E.A., Fuller S.L., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA   Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA   Grunwald N.J., Chang J.H.;
RT   "Evolutionary transitions between beneficial and phytopathogenic
RT   Rhodococcus challenge disease management.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:OZC99288.1}.
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DR   EMBL; NOYI01000024; OZC99288.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A260B7H5; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000215839; Unassembled WGS sequence.
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   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; 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   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   Pfam; PF13193; AMP-binding_C; 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:OZC99288.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          36..89
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          96..462
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          528..601
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   648 AA;  69928 MW;  4B083A8909F0D470 CRC64;
     MISALWTPTD ADVAEARVTE FARFVEQRHD VELPDYEALW RWSTIELESF WRAVWDFFEI
     RAVSDPTTVL ESRTMPGAQW FPGTELNYVD QVIGHARPDR AAIVHAREDG STRIVTWDDM
     IDQAGALAGT LADNGVRRGD RVVGYLPNIP EAVIAFLATA SLGAVWSACG QDYSASAARD
     RLGQLEPTAL ITASGYQYGG QFRDKSGDVA ALVDALPTVR VVVTIGEPTG SARSWSDATA
     ESRELTPAAV PFDHPLWVVF SSGTTGLPKG IVHGHGGVVL EHLKSVALQS DLGPEDVFFW
     YTSPSWMMWN FQIAGLLTGA TIVCADGNPA FPMPDALWDI AGRLGVTYLG TSPGYVLACI
     KAGTHPGADH DLSALRAVGI TGSAMPASSS IWLSENIGAH VPVFSISGGT DVVSAFAGGV
     RTAPVWAGEL SVPFLGVALD AYDEDGEPVR GTVGELVVTE PMPSMPLYFW NDADGSRYRA
     AYFDTYPGIW RHGDWITLTD RGSVVVHGRS DSTLNRNGIR MGSADIYQAV ESLDEVTEAL
     VLGIELPDGQ YWMPLFVVVP DGLTDELHAR IESVIRTQAS PRHVPDDIVA TPAIPHTRTG
     KKLEIPLKRL FQGAAAAGTL DASAVDDPAA LAWFVDRATE FQRVQRAR
//
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