ID A0A2C1KYA5_9BACI Unreviewed; 570 AA.
AC A0A2C1KYA5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=COD11_01535 {ECO:0000313|EMBL:PGT91192.1};
OS Bacillus sp. AFS040349.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT91192.1, ECO:0000313|Proteomes:UP000222674};
RN [1] {ECO:0000313|EMBL:PGT91192.1, ECO:0000313|Proteomes:UP000222674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS040349 {ECO:0000313|EMBL:PGT91192.1,
RC ECO:0000313|Proteomes:UP000222674};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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:PGT91192.1}.
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; NUMC01000007; PGT91192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1KYA5; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000222674; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05969; MACS_like_4; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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 PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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:PGT91192.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000222674}.
FT DOMAIN 51..409
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 469..547
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 570 AA; 64511 MW; 95D559FB3DE9EBF4 CRC64;
MKLEALPVTK GNYNLTDYDT TYNSFDWSEV EKNFTWSETG RVNAAYEAID KHVETFRKNK
VALYYRDPER DEKYTFKELK ELSNKAANVL KDKADVVKGD RLFVFMPRTP ELYSVILGAI
KLGAIVGPLF EAFMEGAVRD RLEDSDAKVI VTTPELLDRV PVNELPSLKH VVVVGETVDD
SHIDLLTEMK TASKELEIEW MEKTDGLLLH YTSGSTGKPK GVLHVHGAMV QHYQTAQWVL
DLKEDDVYWC TADPGWVTGT VYGIFGPWLS GATNVIVGGR FKPESWYQTI EDYGVTVWYS
APTAFRMLMG AGDELVKQFN TSTLRHVLSV GEPLNPEVVR WGVKVFNNRI HDTWWMTETG
AQLICNYPCM EIKPGSMGKP IPGVEAAIVD DQGNELPPYR MGNLAIKKGW PSMMHTIWNN
QEKFESYFMP GDWYVSGDSA YMDEDGYFWF QGRIDDVIMT SGERVGPFEV ESKLVEHPAI
AEAGVIGKPD PVRGEIIKAF VALREGYEPT DELKEEIRTF VKKGLAAHAA PREIDFRDKL
PKTRSGKIMR RVLKAWELDL PTGDLSTMED
//