ID A0A0W0SUT3_9GAMM Unreviewed; 622 AA.
AC A0A0W0SUT3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN Name=acsB {ECO:0000313|EMBL:KTC87001.1};
GN ORFNames=Lbru_0230 {ECO:0000313|EMBL:KTC87001.1};
OS Legionella brunensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=29422 {ECO:0000313|EMBL:KTC87001.1, ECO:0000313|Proteomes:UP000054742};
RN [1] {ECO:0000313|EMBL:KTC87001.1, ECO:0000313|Proteomes:UP000054742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43878 {ECO:0000313|EMBL:KTC87001.1,
RC ECO:0000313|Proteomes:UP000054742};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
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:KTC87001.1}.
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; LNXV01000003; KTC87001.1; -; Genomic_DNA.
DR RefSeq; WP_058440342.1; NZ_LNXV01000003.1.
DR AlphaFoldDB; A0A0W0SUT3; -.
DR STRING; 29422.Lbru_0230; -.
DR PATRIC; fig|29422.6.peg.238; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000054742; 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}.
FT DOMAIN 12..58
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 63..442
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 502..580
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 622 AA; 68758 MW; 2780ACB779374896 CRC64;
MTSQQAISGK DSLENFWADI AHRYVSWIKP WDKTLQGNFT NGDIQWFSGG KLNISANCLD
KHLPNKAEQT AIIWESDDEQ QQRKLSFGEL HQEVCLMANA LKSLGISKGD RVGIYLPMIP
EAAIAMLACA RIGAVHTVVF AGFSPTALRQ RLEAAACKLL ITTDGYNRGG KHFALKQQAD
EATKGLSLQT LVIQHSRESV PFHAKTDHWW HDLKSRVNAD CPPEPMDAEA PLFILYTSGS
TGKPKGVVHT TGGYLVQVAY SHNHIFKCST NEVFWCTADV GWITGHSYVV YGPLCNGITS
LIFAGIPSWP DPARFWNIID KHQVNVFYTA PTAIRALKRA GDQWLTTTNR KSLRMLGTVG
EPINPEVWQW YHDQVGQDRC PIVDTWWQTE TGAIMICPQE DLNAAKPGAA SQPLPGIFPV
LLDEQGKEIK GEGEGSLPIK YPWPSIARTI AGDHERYCET YFNNGYYITG DGAKRDTDGD
YWITGRIDDV LNVSGHRLGT AEIESALVAH PKVAEAAVVG IPHEIKGQGI HAFVSLKTGE
QPSQQLYEEL IDTIKTDIGA IAKPDAISWV NDLPKTRSGK IMRRILRQIA SKDVQDLSEL
GDLSTLANPQ VVNDLMKDHS AS
//
