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Database: UniProt
Entry: C1B2F2_RHOOB
LinkDB: C1B2F2_RHOOB
Original site: C1B2F2_RHOOB 
ID   C1B2F2_RHOOB            Unreviewed;       535 AA.
AC   C1B2F2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=2,3-dihydroxybenzoate-AMP ligase {ECO:0000313|EMBL:BAH50576.1};
DE            EC=6.3.2.- {ECO:0000313|EMBL:BAH50576.1};
GN   OrderedLocusNames=ROP_23290 {ECO:0000313|EMBL:BAH50576.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH50576.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH50576.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH50576.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AP011115; BAH50576.1; -; Genomic_DNA.
DR   RefSeq; WP_012689532.1; NC_012522.1.
DR   AlphaFoldDB; C1B2F2; -.
DR   STRING; 632772.ROP_23290; -.
DR   KEGG; rop:ROP_23290; -.
DR   PATRIC; fig|632772.20.peg.2426; -.
DR   HOGENOM; CLU_000022_59_7_11; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000002212; Chromosome.
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; 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:BAH50576.1}.
FT   DOMAIN          37..398
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          449..524
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   535 AA;  57041 MW;  A37A205320B3C903 CRC64;
     MSENTDHRVG FVPFPDADSD RYRACGYWRG EPLGDILRRA AHRWPQRPAI LADDTTTYAQ
     LDSAADRMAS GLMRMGFAPG DRVVVQLPNV PEFAVVFFGL LRAAAIPVLC LPAHREREIG
     HLAALSGAIG YVVADRVGGY DYRELARAVR AAAPSVEHVL VHGDAREFTS LASVPATVRE
     LPTVDPADVA VLLISGGTTG VPKLIARTHD DYAYNARASA EVCALTGDDV YLVALPAAHN
     FPLACPGILG TFGVGGAVTF LADPSPESAF AAIERHRATV TAVVPPLAQL WCTATEWESA
     DPGSLRLLQV GGAKLAENAA REVRPRLGAA LQQVFGMAEG LLNYTRLDDP DDLVATSQGR
     PLSELDEVRI VDDAGNDVPA GTEGELLTRG PYTIRGYYRA AEHNARAFTA DGFYRSGDLV
     RRLPSGHLVV TGRIKDVINR GGESVSAGEV EEHLLAHPAV VQVAVIGLPD DDLGERVCAA
     MVVDDTLPTL AQLKDFLTGR GLAPFKHPDL LHVVEHLPVT AVGKIDKRAV AADIG
//
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