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Database: UniProt
Entry: A0A1E4J0D9_9BURK
LinkDB: A0A1E4J0D9_9BURK
Original site: A0A1E4J0D9_9BURK 
ID   A0A1E4J0D9_9BURK        Unreviewed;       667 AA.
AC   A0A1E4J0D9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acetoacetate--CoA ligase {ECO:0000313|EMBL:ODU15887.1};
GN   ORFNames=ABS94_15270 {ECO:0000313|EMBL:ODU15887.1};
OS   Variovorax sp. SCN 67-85.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1660152 {ECO:0000313|EMBL:ODU15887.1, ECO:0000313|Proteomes:UP000094461};
RN   [1] {ECO:0000313|EMBL:ODU15887.1, ECO:0000313|Proteomes:UP000094461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(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:ODU15887.1}.
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DR   EMBL; MEFM01000020; ODU15887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4J0D9; -.
DR   Proteomes; UP000094461; 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:ODU15887.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          27..83
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          92..482
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          549..624
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   667 AA;  73475 MW;  361511E26D0263F4 CRC64;
     MSAPNIPQIR LYQNWLREKH GLSFDSYDAL WRWSTTELDA FWRSIWDYAA IQSPTPLASG
     ATVLAERRMP GAQWFPGAQV NYAREVLRHV DAAHAAGMPA IVSDNERGDV REMSWPEMRR
     QVASVALTLR ALGVRRGDRV AAYMPNVPET MVAFLACSSI GAVWSVCAPD MGTAAVADRF
     RQIEPKVLIA VDGVHYGGKP LDRSAVLQEL RGQLPSVKKL VLVKSPFAAN AVPHDIDWSR
     AIGRYDDEVN AFEPEWLPFD HPIWIVYSSG TTGLPKPIVH GQGGIILTMH ACGLHNDVGA
     SYGANNLGER YHWYSSTGWV MWNSQLSGMA FGATICIYDG NPAGSKEKPD WSVLWRFVAR
     HKVTFFGAGA AYFTNCMKAG LVARDCGDLS AVRALGSTGS PLPEEVQRWG SRQILDAGSS
     EVWWCNISGG TDFCGAFVGG NRDLPEVPGQ MQCRELGHAV EAWNDDGQPV IGEVGELVCT
     QPIPSMPLYF WGDEGNARYL SSYFDTYPGV WRHGDWIRIG TDGGCIIYGR SDATINRQGL
     RMGTSEIYSA VEGLPEVLDS MVVDLEYLGR DSYMPLFVVL RPGVALDDGM RARLNNAIKT
     SLSPRFVPND IFQVPEIPRT LSGKKQELPI KKLLLGQPLE KVVNREAMAN PGSLEWYVAF
     AAERASA
//
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