ID A0A0A7JQF3_9PSED Unreviewed; 629 AA.
AC A0A0A7JQF3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:AIZ33154.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:AIZ33154.1};
GN Name=prpE {ECO:0000313|EMBL:AIZ33154.1};
GN ORFNames=NJ69_09250 {ECO:0000313|EMBL:AIZ33154.1};
OS Pseudomonas parafulva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157782 {ECO:0000313|EMBL:AIZ33154.1, ECO:0000313|Proteomes:UP000030632};
RN [1] {ECO:0000313|EMBL:AIZ33154.1, ECO:0000313|Proteomes:UP000030632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRS01-1 {ECO:0000313|EMBL:AIZ33154.1,
RC ECO:0000313|Proteomes:UP000030632};
RA Liu Q.;
RT "Genome sequence of Pseudomonas parafulva CRS01-1, an antagonistic
RT bacterium isolated from rice field.";
RL Submitted (OCT-2014) 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; CP009747; AIZ33154.1; -; Genomic_DNA.
DR RefSeq; WP_039578335.1; NZ_CP009747.1.
DR AlphaFoldDB; A0A0A7JQF3; -.
DR KEGG; ppv:NJ69_09250; -.
DR Proteomes; UP000030632; Chromosome.
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 Ligase {ECO:0000313|EMBL:AIZ33154.1}.
FT DOMAIN 3..56
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 67..444
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 509..588
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 629 AA; 68304 MW; 778AC371B7129210 CRC64;
MTYQHSYAQS IADPARFWQA QADSLAWYRT PSVTLQTNAD GTQRWFADGR LNSSYLALDR
QIELGRGEQV ALIYDSPVTG VTQRFTYSQL RDEVARLAGL LCELGVGKGD GVIIYMPMVP
QAAMAMLACA RIGAVHSVVF GGFAANELAL RIDDARPALV LTASCGLEFD RVIEYKPLVD
RALLLARHQP RHVVVLQRPQ ATAALEPGRD LDWEAAVAGA QSVAPVVLDA GDPLYIMYTS
GTTGKPKGIV RENGGNAVAL CYAMRHVYGM QAGDVWWGIS DVGWVVGHSL IVYGPLMCGC
TTVLYEGKPI RTPDAAAYWR IVEQYRVNGL FCAPTAMRAI RKEDPHGEGV RSHDLSSLRQ
LFLAGEKLDS ATHEWLEGVT GKPVHDHWWQ TETGWPVTAP CVGLEGSAAR PGSSNRAVPG
YHVQVLDDEG RPVAANQQGA IVIALPLPPG CSQTLWGDHS RYVQAYLQRY PGYYHTGDGG
YLDDEGFVYI MGRTDDVINV SGHRLSTGEM EDLVAQHPAV AECAVIGVHD EIKGQVPLAL
VVLKDGQGIG EQQVQAELVA SVREQIGALA CFQRVRVVKR LPKTRSGKIL RAVLRKIADG
QDYVPPSTLD DVAVLGEIEQ VLAGLPRAG
//