ID A0A069IGZ6_9BURK Unreviewed; 630 AA.
AC A0A069IGZ6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:KDP88832.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:KDP88832.1};
GN Name=prpE {ECO:0000313|EMBL:KDP88832.1};
GN ORFNames=CF70_028160 {ECO:0000313|EMBL:KDP88832.1};
OS Cupriavidus sp. SK-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP88832.1, ECO:0000313|Proteomes:UP000023560};
RN [1] {ECO:0000313|EMBL:KDP88832.1, ECO:0000313|Proteomes:UP000023560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-3 {ECO:0000313|EMBL:KDP88832.1,
RC ECO:0000313|Proteomes:UP000023560};
RA Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT "Cupriavidus sp. strain SK-3.";
RL Submitted (MAY-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:KDP88832.1}.
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DR EMBL; JFJV02000035; KDP88832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A069IGZ6; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000023560; Unassembled WGS sequence.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IEA:InterPro.
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 InterPro; IPR012694; Propion_PrpE.
DR NCBIfam; TIGR02316; propion_prpE; 1.
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:KDP88832.1}.
FT DOMAIN 5..58
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 60..446
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 511..594
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 630 AA; 68643 MW; 3E457434E692A9E5 CRC64;
MTATRALHAR SVSDPEGFWA EQARRIDWET PFETVLDDSR PPFARWFVGG RTNLCHNAVD
RHLAARADQP ALIYVSTETG QHRTYSYAEL HDEVNRMAAI LQQMGVVKGD RVLIYMPMIP
EAAFAMLACT RIGAIHSVVF GGFASVSLAA RIDDAQPRVI VSADAGSRAG KVVPYKPLLD
EAVTLAAHKP ERVLLVDRQL APMALTPGRD EDYAAWRERV GAARVPCVWL ESSEPSYVLY
TSGTTGKPKG VQRDTGGYAV ALATSMDYIF CGKAGDTMFS SSDIGWVVGH SYIVYGPLLA
GMATLMYEGT PVRPDGGILW QLVEQYRVNI MFSAPTAIRV LKKQDPAWLT RYDLSSLRLL
FLAGEPLDEP TASWIQQGIG KPVVDNYWQT ETGWPIIAIQ RGIEPLPAKL GSPGVPVYGY
DLKIVDEATG AECAPGQKGV VAIDGPLPPG CMTTVWGDDE RFVKTYWSGV PGRRCYSTFD
WGVQDEDGYI FILGRTDDVI NVAGHRLGTR EIEESISSHP AVAEVAVVGV HDALKGQVAM
AFVIARDAGR IETQADRLAL EGDVMKTVDR QLGAVARPAR VFFVNALPKT RSGKLLRRAM
QAVAEGRNPG DLTTIEDPTA LAQLQAAMQG
//
