ID A0A1L9BSY5_9RHOB Unreviewed; 630 AA.
AC A0A1L9BSY5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:OJH45309.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:OJH45309.1};
GN Name=prpE {ECO:0000313|EMBL:OJH45309.1};
GN Synonyms=yahU {ECO:0000313|EMBL:OJH45309.1};
GN ORFNames=IE00_06600 {ECO:0000313|EMBL:OJH45309.1};
OS Paracoccus sp. SM22M-07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1520813 {ECO:0000313|EMBL:OJH45309.1, ECO:0000313|Proteomes:UP000183790};
RN [1] {ECO:0000313|EMBL:OJH45309.1, ECO:0000313|Proteomes:UP000183790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM22M-07 {ECO:0000313|EMBL:OJH45309.1,
RC ECO:0000313|Proteomes:UP000183790};
RA Carlos C., Ottoboni L.;
RT "Draft sequencing and comparative genomics of Paracoccus sp. SM22M-07
RT isolated from coral mucus: Insights into bacteria-host interactions.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJH45309.1}.
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; JPKW01000003; OJH45309.1; -; Genomic_DNA.
DR RefSeq; WP_072296261.1; NZ_JPKW01000003.1.
DR AlphaFoldDB; A0A1L9BSY5; -.
DR STRING; 1520813.IE00_06600; -.
DR Proteomes; UP000183790; Unassembled WGS sequence.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Ligase {ECO:0000313|EMBL:OJH45309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183790}.
FT DOMAIN 3..56
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 60..443
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 509..587
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 630 AA; 67410 MW; B7F2DED780437F19 CRC64;
MAYRDIYSQW QSDPEGFWMG ASRAIDWTRS SSRAFFDQGP VGEWFADGMV NTCWNAIDRH
VAAGHGDRIA VIHDSAMTGQ VARMTYAELQ DRVARLAGVL AAHGVGMGDR VIIYMPMIPE
ALQAMLACAR IGAIHSVVFG GFAAHELAVR IDDAQPKAIL AASCGLEPNR TVPYKPLLDK
ALDEARHKPG LCVVHQRPEC TADMTPGRDL DWDAAVASAT PVDCVPVAGN HPAYILYTSG
TTGQPKGVVR HTAGHLVALA WSVPQIYDIG PGDVFFVASD VGWVVGHSYI VYGPLIAGAT
TVIFEGKPVG TPDAGTFWRI VADHKVKSFF TAPTAIRAVK RDDPQGGLIG NYDLSSLRAL
FLAGERADPD TITWAEHHLK VPVIDHWWQT ETGWPIAANP LGAGLLPVRK GSPSVPMPGY
AVHVLDEAGH PVAPGTLGAI ALKLPLPPGT LPTLWNAEDR FRKAYLDHFP GYYETGDAGF
VDDDGYVFIM ARTDDVINVA GHRLSTGAME EVLSAHPAVA ECAVIGVADP LKGQAPVGLL
CLKKGVTATS QQVMTEVVAM VRDRIGPVAA FKTACVVDRL PKTRSGKILR ATMAKIADGE
EVKTPATIDD PAILDEIRAA LAGVGYPCKR
//
