ID A9BQN2_DELAS Unreviewed; 704 AA.
AC A9BQN2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Acetoacetyl-CoA synthase {ECO:0000313|EMBL:ABX32734.1};
GN OrderedLocusNames=Daci_0087 {ECO:0000313|EMBL:ABX32734.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX32734.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX32734.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000884; ABX32734.1; -; Genomic_DNA.
DR AlphaFoldDB; A9BQN2; -.
DR STRING; 398578.Daci_0087; -.
DR KEGG; dac:Daci_0087; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_3_3_4; -.
DR Proteomes; UP000000784; Chromosome.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT DOMAIN 46..100
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 108..454
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 581..658
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 704 AA; 76717 MW; B4E71891E83DF3E8 CRC64;
MAFPSGLAGS ARVPWPVMSH TPAFIPQIRL YQDWLRERHG LQFDSYDALW RWSVTDLDAF
WQSIWDYNAL QSPTPHTAVL ERNTMPGAQW FPGAQINYTR QALRHVDAAH AAGMPAVVSR
NETGRHRELS WPELRRQVAA LALHLKAQGV GRGDRVAAYL PNIPEAMVAL LATASLGAVW
SICAPDMGTN AVLDRFRQIA PKALIAVDGV HYAGRDIDRM AVLAELRAGL PSVEHVVLVP
NLDLQARLAD AADYGQVTAR DDAATAAFEP EWLPFDHPLW IVYSSGTTGL PKPIVHGHGG
MVLVALQLKA LHNDVGCSYH PNSWGERYHW YSSTGWVMWN AQVSGLLGGT TCVIFDGSPG
GSKDRPDWGV LWRFAAETGV TSFGSGAAFY ANCMKAGVDL AQCGDLSRIR SLGTTGSPLS
PEVQSWGTAQ FAGMGRPDIW WNNISGGTDF AGAFIGGHRE LPQQPGIMQC RQLGAAVEAW
NEQGQPVIDE VGELVCTQPI PSMPLYLWGD ADGKRYLSSY FDMYPAGHGR APGGGDGPAA
MGPVWRHGDW IRILPEGGCI IYGRSDATIN RHGLRMGTSE IYSAVEALPE VLDSMVVDLE
YLGRESFMPL FVVLRPGVDL DDALRARLQG AIRQALSPRF VPDEIVQVAE IPRTLSGKKQ
ELPIKKLMLG QPLDKVVNKE AMANPGCLDW YVGFAAQHAK AQAA
//
