ID C0ZQ73_RHOE4 Unreviewed; 534 AA.
AC C0ZQ73;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Putative fatty-acid--CoA ligase {ECO:0000313|EMBL:BAH31551.1};
DE EC=6.2.1.- {ECO:0000313|EMBL:BAH31551.1};
GN OrderedLocusNames=RER_08430 {ECO:0000313|EMBL:BAH31551.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31551.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
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-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH31551.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH31551.1; -; Genomic_DNA.
DR RefSeq; WP_020906239.1; NC_012490.1.
DR AlphaFoldDB; C0ZQ73; -.
DR KEGG; rer:RER_08430; -.
DR PATRIC; fig|234621.6.peg.1297; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_11; -.
DR Proteomes; UP000002204; 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; PTHR43201:SF36; 2-SUCCINYLBENZOATE--COA LIGASE, CHLOROPLASTIC_PEROXISOMAL; 1.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 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:BAH31551.1}.
FT DOMAIN 48..395
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 444..517
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 534 AA; 57520 MW; EB9B6779E482317B CRC64;
MTTTQAARSA TSKSERWGSD IEPVTVGDLT FRMYSERPHR LGSLLTFASR WGDRAHIVQG
ERVVTFEQFR ASVDARAHEF TSAGIGSGDR VVLLGFNSPE WIVNFWATVA VGGVAVLANA
WWSEEELVSS LELVEPVLVL ADERIASRVP DRYKVATWSP TADPSPTAAT PFVDPGTAEE
DPAVVIFTSG TSGKPKGVVL SHRSLLSGLQ MLLDITRRLP HLVDETAGES ALHTGPMFHV
GGVQTLLRAI CVGDTLVMPA GRFDPAEAIR LVEDWKIRRW SAVPTMVTRV LEHPDVRTRD
LTTLRAVTVG GAPVGAEFLE RLRTGLPGVE PRVATGYGLT ENGGQGVAAS GKDTVKHPGT
TGRALPCVEI SIAPRPELPD GEILLRSPTQ MLGYLGEIES PIDSDGWLHT GDLGHLDDEG
YLWITGRSKD MIIRGGENIA PASVEAALVR LPEVKDAVVF GVPHSDLGEE VAAALVLESD
VDPTQFGDRL RGTIASFAVP TRWIVVTEDF PVNHAGKIDK NAVVADARTK VESR
//
