ID A0A0M2GKU0_9ACTN Unreviewed; 539 AA.
AC A0A0M2GKU0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:KJK36356.1};
GN ORFNames=UK15_26545 {ECO:0000313|EMBL:KJK36356.1};
OS Streptomyces variegatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK36356.1, ECO:0000313|Proteomes:UP000034786};
RN [1] {ECO:0000313|Proteomes:UP000034786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJK36356.1}.
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DR EMBL; JYJH01000022; KJK36356.1; -; Genomic_DNA.
DR RefSeq; WP_031141365.1; NZ_JYJH01000022.1.
DR AlphaFoldDB; A0A0M2GKU0; -.
DR STRING; 284040.UK15_26545; -.
DR PATRIC; fig|284040.3.peg.3673; -.
DR Proteomes; UP000034786; Unassembled WGS sequence.
DR GO; GO:0016877; F:ligase activity, forming carbon-sulfur bonds; IEA:UniProt.
DR CDD; cd05924; FACL_like_5; 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; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 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;
FT DOMAIN 10..384
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 448..524
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 539 AA; 58410 MW; FAFB48DE7B076E81 CRC64;
MEYNLADLFE SVVDVVPDRE ALVYADHPGT GAERRLTYAE LDAAADRVGH HLLDSGIRPG
EHVGLHLYNG VEYLQTVLGC LKARIVPVNV NYRYVEEELV YLYRDADLVG LVFDAEFTDR
VAAARPRAGK LRHLIRVGAA APGAAEVPCV EFAQVEAAGS PERGFPARSA DDQFIIYTGG
TTGMPKGVMW RQEDLFFAGL GGGAPTGEPV KKPEELAERV AAGGAGITFF PTAPLMHGTS
TLTAFIGFNF GQRVVIHRKF VPDEVLRTVE KERVSSISLV GDAMLRPLVD ALSGPLRHID
RSSLFSVSSS GAILSDTVRR QFQELVPNAM LLNNFGSSES GFNGTATEDS GPERGFRVRV
NARTQVVDPA TYAPVAAGEV GRIAQCGHVP LGYYNDPAKT AGTFFERDGE RWVLLGDMAT
VDEEGVVTVL GRGSQCINTG GEKVYPEEVE QALKSHPDVY DALVAGVPDP RWGHQVAAVV
QLREGAARPS LEDIRTHCRD RLAGYKIPRR LVITESIQRS PSGKADYRWA REVAVTADG
//