ID C0ZN99_RHOE4 Unreviewed; 539 AA.
AC C0ZN99;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative fatty-acid--CoA ligase {ECO:0000313|EMBL:BAH31151.1};
DE EC=6.2.1.- {ECO:0000313|EMBL:BAH31151.1};
GN OrderedLocusNames=RER_04430 {ECO:0000313|EMBL:BAH31151.1};
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:BAH31151.1, 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:BAH31151.1, 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).
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DR EMBL; AP008957; BAH31151.1; -; Genomic_DNA.
DR AlphaFoldDB; C0ZN99; -.
DR KEGG; rer:RER_04430; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_7_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; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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:BAH31151.1}.
FT DOMAIN 23..376
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 428..502
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 539 AA; 58667 MW; 36786D686F358577 CRC64;
MLSATRPRAM TGGGVLPEML LDALRRDPEA LALVDESVRW TYQELVDAAT SFAGALHKSG
FEPGEVVLVQ LPNWWESVVA AWGTWLAGGI LLPVVPIYRA HELSFIIEQA EPSVIVAPQE
YRGYRHVEQL GTVLRDLGRE VLLVEARGEG GLRRTTFDDF LDFGMEANRP DHRADPDDVA
LVLYTSGTTS APKGVLHTHR TLMAESSSMI AHCGVDSQDR IFMPSPLPHI TGMSYAVVLP
AAAACSTVLM QRWNPAEAVA LIEREQCTFT VSATPFLRGL ADAYEEDGYR RSHLTRFVCG
GAGIPPELVR RAHRVMGTAV VRTYGSTELP TLVMGDPFGD IGLQAEDEGA VIGGNEFRLG
EDDELLVRGP ELFVGYVDSS INAESFTEDG YFRTGDVATV DGPGQIRITS RIKDIINRGG
EKFSAADIEW VLEAHPNVAE VAVVGYPDEE LGERACAFVV PHGEPPSVRD LRIFLLSEGF
AVQKAPERVE TVASLPRTES GKVQKFLLRR ALGLGSAQAV PETYGSEFGH DGNRRKATS
//
