ID J3CH72_9BURK Unreviewed; 686 AA.
AC J3CH72;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Acetoacetyl-CoA synthase {ECO:0000313|EMBL:EJL71351.1};
GN ORFNames=PMI12_04346 {ECO:0000313|EMBL:EJL71351.1};
OS Variovorax sp. CF313.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1144315 {ECO:0000313|EMBL:EJL71351.1, ECO:0000313|Proteomes:UP000007277};
RN [1] {ECO:0000313|EMBL:EJL71351.1, ECO:0000313|Proteomes:UP000007277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF313 {ECO:0000313|EMBL:EJL71351.1,
RC ECO:0000313|Proteomes:UP000007277};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL71351.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKIW01000085; EJL71351.1; -; Genomic_DNA.
DR RefSeq; WP_007836498.1; NZ_AKIW01000085.1.
DR AlphaFoldDB; J3CH72; -.
DR PATRIC; fig|1144315.3.peg.4287; -.
DR Proteomes; UP000007277; 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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 51..104
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 116..491
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 75108 MW; AEDD8AC16129A577 CRC64;
MTTHPEIAPH AVSAPSDAPL WTPTPARKER ALITRFEAWL DRERGLRFEN YEALWQWSVT
DLEGFWSAVL AFFELPLRAP YESVLSGEDM PGARWFEGAR LNLVDQVFRH ARLASPAIVF
ESEASGTGAM SWVELQRQVA SVAQALRDLG VQQGDRVAGY LPNIPQAVVA FLAAASLGAV
WSLCAPDMGP VSVGDRFRQI EPKVLVAVDG YRFGGKPFDR RGALDEILRE LPTVTGILWI
PHLDAAAHPP GQAAGRTTVR WQEAIAREAA WQPAALPADH PLWILYSSGT TGLPKAIVHG
HGGVLANGMV NMVLHGDLHP GERVFWAANT SWMVWNAHVL GLLGGATLVL YDGAVTGAGA
EPDWGHLWKL AGRLGVHVFG AGAAIHHACL KAGIVPREIA DLGQLHTVSS TGSPLSPEAC
EWLYGAVKRD LWLNIVSGGT DIAGGFLVGL PTLPVRTGEM QCRTLGACVQ AWNDAGQPVL
DEVGELVCTR PLPSMPLYFW GDAGHRRYLD SYFESFKDSQ GRNVWRHGDW VRLVPRPDAT
AGVIYGRSDA TINRQGVRMG TSELYRVVQG MAEVMDSLVV DLEYLGRDSY MALFVQLQAG
IQLDEPLEQR IRQALRTGLS ARHVPNEIIQ VDTIPKTITG KKLELPVKKL LLGHALEKVV
SRNALAEPGS IDWYVDFAER YRRRTG
//
