ID G2EGW7_9FLAO Unreviewed; 635 AA.
AC G2EGW7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN Name=acs {ECO:0000313|EMBL:EGV42329.1};
GN ORFNames=BZARG_2584 {ECO:0000313|EMBL:EGV42329.1};
OS Bizionia argentinensis JUB59.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV42329.1, ECO:0000313|Proteomes:UP000003730};
RN [1] {ECO:0000313|EMBL:EGV42329.1, ECO:0000313|Proteomes:UP000003730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUB59 {ECO:0000313|EMBL:EGV42329.1,
RC ECO:0000313|Proteomes:UP000003730};
RX PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA Memoli M., Arguelles M., Mac Cormack W.P.;
RT "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT Antarctica.";
RL Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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:EGV42329.1}.
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DR EMBL; AFXZ01000065; EGV42329.1; -; Genomic_DNA.
DR RefSeq; WP_008639350.1; NZ_AFXZ01000065.1.
DR AlphaFoldDB; G2EGW7; -.
DR STRING; 1046627.BZARG_2584; -.
DR PATRIC; fig|1046627.3.peg.2745; -.
DR eggNOG; COG0365; Bacteria.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000003730; Unassembled WGS sequence.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:EGV42329.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003730}.
FT DOMAIN 12..68
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 73..462
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 519..598
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 635 AA; 71801 MW; F6EAA46C922817D7 CRC64;
MSNYHIKHLE EYYQIYRKSI REPENFWEEV AEEHFVWRKK WDKVLSWDFS KPEIKWFEGA
KLNITENCID RHLVTRGNKT AILFEPNNPD EPAEHISYNE LHERVNQMAN VLKDHGIKKG
DRVCIYVPMI PELAISILAC ARIGAIHSVV FAGFSSTALS TRINDSDCKM VIAADGSYRG
AKTIDLKGIV DEALESCPGV ESVLMVKRIN SDIKMKKGRD KWLQPLLDEA STQCPAEIMD
AEDPLFILYT SGSTGKPKGM VHTTAGYMVY TAYSFKNAFQ YRENDVYWCT ADIGWITGHS
YIVYGPLANG ATTVLFEGIP SYPDFGRFWD IIDKHKVNQF YTAPTAIRAL AKQGSELVEK
FDLSSIKVLG SVGEPINEEA WHWYNDNIGK NKSPIIDTWW QTETGAIMIT PIPYVTPTKP
TYATLPFIGV QPAIVNEAGE ELKGNQVEGR LCIKFPWPSM ARTIWRDHKR YKETYFSTVK
NMYFTGDGAL RDEVGYYRIT GRVDDVIIVS GHNLGTAPIE DAINEHPAVA ESAIVGFPHE
IKGTALYGYV TLKDAGEGRI HDNVRKEINQ LITERIGPIA KLDKIQFTQG LPKTRSGKIM
RRILRKIAER DTSNLGDIST LLNPECVQDI IDEAL
//