ID   A0A024H4T8_9MICC        Unreviewed;       609 AA.
AC   A0A024H4T8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Acyl-CoA synthetase {ECO:0000256|ARBA:ARBA00032875};
GN   Name=fadD15 {ECO:0000313|EMBL:CCQ46983.1};
GN   ORFNames=ARTSIC4J27_2961 {ECO:0000313|EMBL:CCQ46983.1};
OS   Pseudarthrobacter siccitolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=861266 {ECO:0000313|EMBL:CCQ46983.1, ECO:0000313|Proteomes:UP000035722};
RN   [1] {ECO:0000313|Proteomes:UP000035722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4J27 {ECO:0000313|Proteomes:UP000035722};
RX   PubMed=24948757; DOI=10.1128/genomeA.00526-14;
RA   Manzanera M., Santa-Cruz-Calvo L., Vilchez J.I., Garcia-Fontana C.,
RA   Silva-Castro G.A., Calvo C., Gonzalez-Lopez J.;
RT   "Genome Sequence of Arthrobacter siccitolerans 4J27, a Xeroprotectant-
RT   Producing Desiccation-Tolerant Microorganism.";
RL   Genome Announc. Announc.2:e00526-e00514(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC         CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00024484};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000256|ARBA:ARBA00024484};
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:CCQ46983.1}.
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; CAQI01000046; CCQ46983.1; -; Genomic_DNA.
DR   RefSeq; WP_050055857.1; NZ_CAQI01000046.1.
DR   AlphaFoldDB; A0A024H4T8; -.
DR   STRING; 861266.ARTSIC4J27_2961; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000035722; Unassembled WGS sequence.
DR   CDD; cd05907; VL_LC_FACS_like; 1.
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; PTHR43272:SF83; ACYL-COA SYNTHETASE LONG-CHAIN, ISOFORM J; 1.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
FT   DOMAIN          49..438
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   609 AA;  64795 MW;  EB5A05CBE6A764AB CRC64;
     MREASTELLV EVDAASNVTD LLLEQESANP ALALYRRKGP NGWVDVPARK FLQDVSALAK
     GLIAGGLEPG DTVAVMSATS YEWTLVDFAI WFAGGVTVPI YETSSASQVE WILHDAGVRR
     VFVEDRSKSQ LVTAVLANSP LLRDRLVNVV RMDSDGEAPN LASLAAAGMG VTDAELERHR
     SKAVLEDVAS LVYTSGTTGK PKGCEITHGN FALVAKNIVA FLPGLLLQEQ ARTLMFLPLA
     HVLARAVQVV CLAAGATLGH SPGAVRLLED LGSFRPTFLL VVPRIFEKVR ATAAHKAAVG
     GKARLFSAAA ATAIEYSRAE DLKSRGEGAG PGLLCRIRHG IFDRLLYPRL RQAMGGQVGY
     TVSGASPLRL EDAHFFRGAG IPVLEGYGLT ETTAPCTANT PTRTKVGSVG IPIPGTTIRV
     ADDGEILVKG IGVFRGYHAN QAANAEAFVD GFFRTGDLGE LDPQGFLTIT GRKKDLLVTA
     GGKNVAPGPL EEKIRAHQLV GHAVVVGDGK PFISALVTLD PEGLENWHSE RGLPSRTIRE
     AAADPEVAAA VQEAVDQANL LVSKAESIRK FTLLDAEFTV ESGHLTPSLK VKRNAVVRDF
     EAEIGKLYT
//