ID A0A075JMC8_9BACI Unreviewed; 524 AA.
AC A0A075JMC8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acyl--CoA ligase {ECO:0000313|EMBL:AIF42522.1};
GN ORFNames=X953_03935 {ECO:0000313|EMBL:AIF42522.1};
OS Virgibacillus sp. SK37.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=403957 {ECO:0000313|EMBL:AIF42522.1, ECO:0000313|Proteomes:UP000027985};
RN [1] {ECO:0000313|EMBL:AIF42522.1, ECO:0000313|Proteomes:UP000027985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK37 {ECO:0000313|EMBL:AIF42522.1,
RC ECO:0000313|Proteomes:UP000027985};
RA Phrommao E., Yongsawatdigul J., Rodtong S., Steele J.L.;
RT "Complete genome sequence of Virgibacillus sp. SK37, a moderately
RT halophilic bacterium isolated from Thai fish sauce fermentation.";
RL Submitted (FEB-2014) 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; CP007161; AIF42522.1; -; Genomic_DNA.
DR RefSeq; WP_040954418.1; NZ_CP007161.1.
DR AlphaFoldDB; A0A075JMC8; -.
DR STRING; 403957.X953_03935; -.
DR KEGG; vir:X953_03935; -.
DR HOGENOM; CLU_000022_59_10_9; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000027985; 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:AIF42522.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027985}.
FT DOMAIN 22..382
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 432..510
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 524 AA; 59160 MW; A620E7AFB7023493 CRC64;
MNREELIAPN DYNIVMEMEK YAKDPSKTAL LWEDEHGNEQ DITYTQLIKN TNKIGNAFLS
SGLSKGDKIL VMIPRLIEAY EVYLAALKTG IIIIPSSEML KTKDLQYRVT HGEVSGVVSY
YPFVDQYNGI NEYEQLKKFV IGKEQDGWLN LDVLKEEASD ELDIAATTRD DIAFLPYTSG
TTGNPKGVVH THGWGYAHFK TAAENWLCIN EGDKVWATAG PGWQKWIWSP FLSVLGSGAT
GFVYNGKFDA KKYLQLLQDK EINVLCCTPT EYRIMAKVEN LDDYQLPALH SAVSAGEPLN
VEVIDTFRKY FNITVRDGYG QTENTLLLGI MKDMEVRPGS MGKPTPGNDV EIINEKGEPA
EIGEVGDIAV KINCPALFKE YYKDDEKTKM SRRGDYYLTG DQASKDKDGY FWFEGRSDDI
IISSGYTIGP FEVEDALVKH PSVQECAVVA SPDKIRGRVV KAFVVLREGV QEDSALVKEL
QDHVKEWTAP YKYPRKIEFL RELPKTTSGK IRRVELRNKE KVKS
//
