ID K0K6F4_SACES Unreviewed; 528 AA.
AC K0K6F4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Acyl-CoA ligase {ECO:0000313|EMBL:CCH32123.1};
GN OrderedLocusNames=BN6_48510 {ECO:0000313|EMBL:CCH32123.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH32123.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH32123.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE804045; CCH32123.1; -; Genomic_DNA.
DR RefSeq; WP_015102235.1; NC_019673.1.
DR AlphaFoldDB; K0K6F4; -.
DR STRING; 1179773.BN6_48510; -.
DR KEGG; sesp:BN6_48510; -.
DR PATRIC; fig|1179773.3.peg.4865; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_7_11; -.
DR OrthoDB; 9803968at2; -.
DR BioCyc; SESP1179773:BN6_RS23470-MONOMER; -.
DR Proteomes; UP000006281; 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; IPR020459; AMP-binding.
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 PRINTS; PR00154; AMPBINDING.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:CCH32123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006281}.
FT DOMAIN 10..388
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 438..516
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 55970 MW; 96DEA930A8F47A3E CRC64;
MSVSVASILA ESAARRPHHT ALVHEGERVD YAELWLRARA HAAVLRERGV GPGDRVALLV
PNHPVFCEVY FAVLALGAVA VPVNVLLTVD EVAFVLADSA AGHVVCAGSL LGVGEPAAER
AGSRVLQVLP TGSGATGSDP NGSDATGSDA GGPDRLDVLA RAAEPIAEHV LRAPDDLALV
LYTSGTTGKP KGAMLTQLNV LLNVGTTMRS PFDMGPDDVL FGCLPLFHTF GQVCGMLTCF
AAGATMVLAA RFAAAPALGL MAEHGCTVFM GVPTMYHDLL AAAGTAPRTP RLHRAYSGGS
ALPVRVLEDV ERVFGCPVYE GYGLTETSPV VAYNQKAWPR RPGTVGRPVW GVRVAIARAE
LDSRVELLPA GEVGEVVISG HNVMAGYLNR PEATAEALVD GWFRSGDLGV LDADGYLRLV
DRKKDMVVRG GFNVYPREVE EVLVRHPQVD RVAVIGVPDE RHGEEVCAVV ALRPGVRGCA
EVAAALTAWS RERLAAYKYP RRFEFVDTFP LGPSGKVLKR ELVSRYAG
//
