ID Q82MQ7_STRAW Unreviewed; 503 AA.
AC Q82MQ7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Acyl-CoA synthetase, long-chain fatty acid:CoA ligase {ECO:0000313|EMBL:BAC69314.1};
GN Name=fadD7 {ECO:0000313|EMBL:BAC69314.1};
GN ORFNames=SAVERM_1603 {ECO:0000313|EMBL:BAC69314.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC69314.1, ECO:0000313|Proteomes:UP000000428};
RN [1] {ECO:0000313|EMBL:BAC69314.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2] {ECO:0000313|EMBL:BAC69314.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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DR EMBL; BA000030; BAC69314.1; -; Genomic_DNA.
DR RefSeq; WP_010983042.1; NZ_JZJK01000086.1.
DR AlphaFoldDB; Q82MQ7; -.
DR KEGG; sma:SAVERM_1603; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_7_11; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0016877; F:ligase activity, forming carbon-sulfur bonds; IEA:UniProt.
DR CDD; cd05936; FC-FACS_FadD_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; 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;
KW Ligase {ECO:0000313|EMBL:BAC69314.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000428}.
FT DOMAIN 12..366
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 416..489
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 503 AA; 53598 MW; 971CAA4E77C1CCD7 CRC64;
MAATLSLAAI LAENARRRPE KTALVEGELR LTFAEVWQRA RAQAGALVGL GVRPGDRVAL
MAPNTADFPH AYYAIAAAGG VVVPVHLLLS ASEVEHVLKD SGATLLLCHP AQAETGTAAA
QAVGVQVITL GAEFEKLARI AEPLPSYVTR AADDPAVVFY TSGTTGVPKG AVLSHFNLVM
NATVNAFDAN DIRPDDVALG ALPLFHAFGQ TVSMNSTWRA GATLVLLPRF DAARAIELMV
KEGVNTFHGV PTMFVALAGA AAAMDALPEL RVCVSGGASL PLAVLERFEE AFGAKIYEGY
GLSETSPTAT VNQPVFGTRA GTIGHPLWGV DVEIARAEVE GRVELLPPGE LGEVVVRGHN
VFSGYLGRPE ATAETLVDGW LRTGDLGTKD DEGFLRIVDR KKDVIIRGGY NVYPREVEEV
LLRHPGVAQA AVIGLPDELH GEEVCAVVVR ATGAVPEAAE ITEWSKEHLG RHKYPRRVEF
TDALPLGPSM KILKRELRVR YAQ
//
