ID A0A0Q6XHS0_9BURK Unreviewed; 640 AA.
AC A0A0Q6XHS0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=ASC87_24065 {ECO:0000313|EMBL:KQV96952.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV96952.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQV96952.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV96952.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV96952.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV96952.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQV96952.1}.
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DR EMBL; LMDI01000020; KQV96952.1; -; Genomic_DNA.
DR RefSeq; WP_056663802.1; NZ_LMDI01000020.1.
DR AlphaFoldDB; A0A0Q6XHS0; -.
DR STRING; 1736433.ASC87_24065; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000051465; Unassembled WGS sequence.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:InterPro.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR CDD; cd05966; ACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
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; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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:UP000051465}.
FT DOMAIN 12..67
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 69..460
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 523..605
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 640 AA; 69419 MW; C7E04AB881884F60 CRC64;
MEDAHVCGMA AYDKLVAEAD ADPSGYWSRL ARELVSWKTP FTKGLDDSQA PFFQWFADGT
LNVSYNCLDR QVERGLGDKT AIIFESDDGT VSRVSYSDML ARTCRLANVL RARGVKKGDR
VVIYMSMSVE GVVAMQACAR IGATHSVVFG GFSAQSLRDR IEGAGAVMVI TADHQLRGGK
QLPLKAIVDE AIALGGCDAV ADVIVYRRTG GAVAWEPSRD RWMHEEMQAQ PPTCEPEWVG
AEHPLFILYT SGSTGKPKGV QHASGGYLLH AALTTKWSFD MKPDDVFWCT ADIGWVTGHT
YIAYGPLALG ATQVVFEGVP TYPDAGRFWK MIQDHQVSVF YTAPTAIRSL IKLAEADATV
HPKRYDLSSL RILGSVGEPI NPAAWAWYHQ HIGGGRCPIV DTFWQTESGG HLITPLPGAT
PLVPGSCTLP FPGITAAIVD EYGNDVPHGQ GGILVIKTPW PSMIRTIWGD PERFKSSYFP
AELKGCYLAG DGAIRDPLTG YFTITGRIDD VLNVSGHRMG TMEIESALVA KTDLVAEAAV
VGRPDDTTGE AICAFVVLKG ARPTGEEATR IANELRNWVA AQIGPIAKPK DIRFGDNLPK
TRSGKILRRL LRSIANGEAI TQDTSTLENP AVLEQLAQKN
//
