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Database: UniProt
Entry: Q0S5S7_RHOJR
LinkDB: Q0S5S7_RHOJR
Original site: Q0S5S7_RHOJR 
ID   Q0S5S7_RHOJR            Unreviewed;       552 AA.
AC   Q0S5S7;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=CoA ligase {ECO:0000313|EMBL:ABG97109.1};
DE            EC=6.2.1.- {ECO:0000313|EMBL:ABG97109.1};
GN   OrderedLocusNames=RHA1_ro05328 {ECO:0000313|EMBL:ABG97109.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97109.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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DR   EMBL; CP000431; ABG97109.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0S5S7; -.
DR   KEGG; rha:RHA1_ro05328; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_2_11; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; PTHR24096:SF149; 4-COUMARATE--COA LIGASE 1-RELATED; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 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:ABG97109.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN          52..412
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          463..538
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   552 AA;  58312 MW;  6C02577E63AAEC56 CRC64;
     MRPAFGHETN SPLLQHFEGE APVSFKSPFP DVEIPNLSVY DFLFGRVDPA DGDRPALIDG
     ASGAVTTYRS LVAQINGVAG ALAARGLAVG EVVGLHSPNV PAFASVFHGI LRAGGVATTI
     NALYTAEDIA KQLTDSKAKF LFTVSPLLPQ AKDAAAKVGI PVANVIVLDG ADGHPSLTDL
     LAERAPAPEV SFDPATQLAV LPYSSGTTGR PKGVMLTHRN LVANVCQINP RMGIGADDTL
     LAVLPFFHIY GMTVLLNAAL YNRASLVTMP KFDLVEFLSI VSGQKCTYVF IAPPVAVALA
     KHPLVDDYDL SSVHSIFSGA APLDQELGKA VANRLGCRVR QGYGMSEMSP VSHAIPFDRD
     DIALDSVGPS IANMECKLVD PATGEEVAYP ADGVSAPGEL WCKGPNIMAG YLGNDEATAE
     TLDADGYLHT GDIATVDSEG VVTIVDRMKE LIKYKGYQVP PAELEALLLT HPQIADAAVI
     GVLDDEGEEV PKAFVVRQPG AELDEAAVIG FVAERVSPHK KVRKVEFIDL VPKSAAGKIL
     RKDLRAAETA GR
//
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