ID A0A0M2PFQ3_9BACI Unreviewed; 527 AA.
AC A0A0M2PFQ3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acyl--CoA ligase {ECO:0000313|EMBL:KKI91670.1};
GN ORFNames=WQ54_13680 {ECO:0000313|EMBL:KKI91670.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI91670.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI91670.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI91670.1,
RC ECO:0000313|Proteomes:UP000034887};
RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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:KKI91670.1}.
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DR EMBL; LATZ01000022; KKI91670.1; -; Genomic_DNA.
DR RefSeq; WP_046517457.1; NZ_LATZ01000022.1.
DR AlphaFoldDB; A0A0M2PFQ3; -.
DR PATRIC; fig|1455638.3.peg.3063; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000034887; Unassembled WGS sequence.
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:KKI91670.1}.
FT DOMAIN 25..382
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 432..511
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 527 AA; 59545 MW; 0EEC3A7D156F6998 CRC64;
MVREELLAPL SYNLVEEFEK YAADSTKVAL LWESEQGEKK EITYRELLQK VNQIGNALIS
EGLKSGDKVL VVIPRVIEAY AVYLGALKAG LVVIPSSEML RTKDLQYRVS HGDVKAVISY
GLYTSEFRQI KEYNNLIKIV VNGNEKDWLS LDDLMANQST TMEIAETTSE SMAFLSYTSG
TTGNPKGVVH THGWAFAHLR TAAKNWLSIN EQDIVWATAG PGWQKWIWSP FLSVLGSGAT
GLVYHGKFDP EKYLLLLDEY KVNVLCCTPT EYRIMAKVEN LENYSLANLH SAVSAGEPLN
REVIDTFKRY YNVKVRDGYG QTENTLLVGV MKEMDIKPGS MGKPTPGNDV IIINDEGEPC
SINEVGDIAV HKDTPALFKE YYKEFERTAM QYRGDYYITG DRAKMDEDGY FWFEGRSDDI
IISSGYTIGP FEVEDALVKH PLVKECAVVA SPDEIRGNIV KAYIVLRDPS HQTNADLIQT
LQNHVKELTA PYKYPREIEF INELPKTTSG KIRRIELRQR ELELKQA
//
