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Database: UniProt
Entry: A0A2S2BRN7_9NOCA
LinkDB: A0A2S2BRN7_9NOCA
Original site: A0A2S2BRN7_9NOCA 
ID   A0A2S2BRN7_9NOCA        Unreviewed;       639 AA.
AC   A0A2S2BRN7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:AWK71297.1};
GN   Name=prpE {ECO:0000313|EMBL:AWK71297.1};
GN   ORFNames=CBI38_06610 {ECO:0000313|EMBL:AWK71297.1};
OS   Rhodococcus oxybenzonivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1990687 {ECO:0000313|EMBL:AWK71297.1, ECO:0000313|Proteomes:UP000245711};
RN   [1] {ECO:0000313|EMBL:AWK71297.1, ECO:0000313|Proteomes:UP000245711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2-17 {ECO:0000313|EMBL:AWK71297.1,
RC   ECO:0000313|Proteomes:UP000245711};
RA   Lee Y., Kim K.H., Chun B.H., Jung H.S., Jeon C.O.;
RT   "Isolation of Rhodococcus sp. S2-17 biodegrading of BP-3.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP021354; AWK71297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2BRN7; -.
DR   KEGG; roz:CBI38_06610; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000245711; Chromosome.
DR   CDD; cd05967; PrpE; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR032387; ACAS_N.
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; PTHR43347; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43347:SF3; ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 3, MITOCHONDRIAL; 1.
DR   Pfam; PF16177; ACAS_N; 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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245711}.
FT   DOMAIN          12..66
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          74..461
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          525..603
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   639 AA;  68542 MW;  3F3DE44EF1DCC204 CRC64;
     MSSPTASAGR TYADVYRESV ERPEEFWLAA ATAVEWVEQP TRALDDSSAP MYRWFPDARL
     NTCFNALDRH VRDGRGDQDA LIYDSAMAPE ASRTYTYAQL LDEVSRFAGV LAAQGVVAGD
     RVIVYMPMIP EAAVAMLACA RIGAVHSVVF GGFAAKELAT RIDDAGPVVL VTASGGLEPG
     RTVEYLPMVA KALELSSTPP HTVIVKNREQ VPGSAADYRN DGASWFDWDA LAADASPVQP
     VPVAATDPLY ILYTSGTTGK PKGVVRDNGG HAVALTWSMT NVYDIGPGDV WWTASDVGWV
     VGHSYIVYGP LLAGATSVLY EGKPVGTPDA GAFWRVISDH GVAALFTAPT AIRAVRKADP
     EAKEIAKYDI SSLKTLFAAG ERLDPDTYAW ATRVLGLPVV DHWWQTETGW AICANLRGLE
     PMPVKAGSPT VPVPGYRVEV VDGEGHVVPA GTEGNIVIGL PLPPGTLTGL WRDPDRFVKS
     YLATFDGYYL TGDSGYIDED GYVFVLGRSD DVINVAGHRL STGSMEAVVA GHPAVAECAV
     VGIRDELKGQ RPSGYVVLKA GVDIDPETLR AELVAMVREQ IGAVATFRDV TVVGALPKTR
     SGKILRKTMR QIADHEPYTV PSTIEDVAVL EALEKQLRD
//
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