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Database: UniProt
Entry: F8IIJ9_ALIAT
LinkDB: F8IIJ9_ALIAT
Original site: F8IIJ9_ALIAT 
ID   F8IIJ9_ALIAT            Unreviewed;       548 AA.
AC   F8IIJ9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:AEJ43331.1};
GN   Name=acs {ECO:0000313|EMBL:AEJ43331.1};
GN   OrderedLocusNames=TC41_1395 {ECO:0000313|EMBL:AEJ43331.1};
OS   Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus acidocaldarius).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ43331.1, ECO:0000313|Proteomes:UP000000292};
RN   [1] {ECO:0000313|EMBL:AEJ43331.1, ECO:0000313|Proteomes:UP000000292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tc-4-1 {ECO:0000313|EMBL:AEJ43331.1,
RC   ECO:0000313|Proteomes:UP000000292};
RX   PubMed=21914900; DOI=10.1128/JB.05709-11;
RA   Chen Y., He Y., Zhang B., Yang J., Li W., Dong Z., Hu S.;
RT   "Complete Genome Sequence of Alicyclobacillus acidocaldarius Strain Tc-
RT   4-1.";
RL   J. Bacteriol. 193:5602-5603(2011).
RN   [2] {ECO:0000313|Proteomes:UP000000292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292};
RA   Chen Y., He Y., Dong Z., Hu S.;
RT   "The complete genome sequence of Alicyclobacillus acidocaldarius sp. Tc-4-
RT   1.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP002902; AEJ43331.1; -; Genomic_DNA.
DR   RefSeq; WP_014464206.1; NC_017167.1.
DR   AlphaFoldDB; F8IIJ9; -.
DR   STRING; 1048834.TC41_1395; -.
DR   KEGG; aad:TC41_1395; -.
DR   PATRIC; fig|1048834.4.peg.1329; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_59_10_9; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000000292; Chromosome.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR   CDD; cd05972; MACS_like; 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; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 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   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEJ43331.1}.
FT   DOMAIN          28..388
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          438..525
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   548 AA;  61271 MW;  B108CBFAE681AB72 CRC64;
     MEPTQTAAFA DLLAPDVFNI AGAILDRDES RRALVWRSET GAKRTLTYGE LRRESLRLAH
     ALHDLGLRKG DRVLVLMPRR PETYAVYLAI LSIGAVVLPG SELLMPNDIA YRLKHAEAKG
     VIAHAALAER AEAAIAEAPW VQLRVVVEGS REGFLAYEDL VRGAPGEWDV VPTRRDDLAF
     LSYTSGTTGY PKGVMHVHGW AYAHWHIAAK RWLGIEPDDV VWATAGPGWA KWIWSPFVAT
     LMSGATGFHY GGRFDAETFL RLIDEEGVNV LCATPTEYRM MAKVDGLDRF RLSSLRQAVS
     AGEPLNREVI DTFRRHFQIT VRDGYGQTEN TLLVATCVDT EVRPGSMGLP TVEGAVDIVD
     EEGRSLPPGQ VGDIAVRRDF PALFRGYYKD EERTVAQFRG AWYITGDRAE KDQDGYLWFS
     GRADDIIISA GYTIGPFEVE DALVKHPLVR ECAAVSSPDE VRGAIVKAFV VLKDLNLHRE
     LASDAERREA LVRELQEHVK RITAPYKYPR AIEFVEDLPK TTSGKIRRVE LREREWKRHR
     ELNAGQGG
//
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