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Database: UniProt
Entry: A0A1Q5L386_9ACTN
LinkDB: A0A1Q5L386_9ACTN
Original site: A0A1Q5L386_9ACTN 
ID   A0A1Q5L386_9ACTN        Unreviewed;       492 AA.
AC   A0A1Q5L386;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:OKJ88327.1};
GN   ORFNames=AMK31_07320 {ECO:0000313|EMBL:OKJ88327.1};
OS   Streptomyces sp. TSRI0107.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ88327.1, ECO:0000313|Proteomes:UP000185813};
RN   [1] {ECO:0000313|EMBL:OKJ88327.1, ECO:0000313|Proteomes:UP000185813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ88327.1,
RC   ECO:0000313|Proteomes:UP000185813};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ88327.1}.
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DR   EMBL; LIVZ01000003; OKJ88327.1; -; Genomic_DNA.
DR   RefSeq; WP_073939591.1; NZ_LIVZ01000003.1.
DR   AlphaFoldDB; A0A1Q5L386; -.
DR   STRING; 1703942.AMK31_07320; -.
DR   OrthoDB; 5240965at2; -.
DR   Proteomes; UP000185813; Unassembled WGS sequence.
DR   GO; GO:0016877; F:ligase activity, forming carbon-sulfur bonds; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000185813}.
FT   DOMAIN          6..349
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   REGION          468..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  51470 MW;  E3B49C9CD96A744F CRC64;
     MLDTLAHALR RHPDRPAVLG TTRSGAERTR ATYGDLADLA DRYTTALHAR GVARGGTVGV
     AVRPGPRALP VMLAVHGLGA RAAVLDPGAG PDVLRARLAL ARPDLVLADA TAQAVAGWAR
     PLARAARLAL PDLAMLGPVA TVGPRMPGCA PALDADVRSV VLPRPVDGDG DAVIVFTSGT
     TSRPRAVVHT RSSLAAGMAT VADLVRPEAG RPVLGGTFFV LVPSLASGAP VALPARSTRV
     LARQLRRLAP QCTYLTPPQL RRLLAEGGRF TGRVWTGSAP ASSELLTRVK RAGADEAWGV
     YALTELFPAA AVEQADKAAF TGDGDLVGAP LPGVTAKTDS DGELLLSGPA ARDRYLGEDP
     DPWVATGDRA RLDGGRIVLE GRRKDMILRR AENIYPGLYE PALHVPGVEL ALLVGVPDDD
     GDERLVAVVQ PAAKADRAAL RSALAEPLER MGAARPDAVL LADIPLSGRS RKPDRAATAR
     LAARRLAERS RR
//
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