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Database: UniProt
Entry: A0A2C1KYA5_9BACI
LinkDB: A0A2C1KYA5_9BACI
Original site: A0A2C1KYA5_9BACI 
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}.
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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
//
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