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Database: UniProt
Entry: A0A0F4RQN8_9RHOB
LinkDB: A0A0F4RQN8_9RHOB
Original site: A0A0F4RQN8_9RHOB 
ID   A0A0F4RQN8_9RHOB        Unreviewed;       630 AA.
AC   A0A0F4RQN8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:KJZ21052.1};
DE            EC=6.2.1.17 {ECO:0000313|EMBL:KJZ21052.1};
GN   Name=prpE {ECO:0000313|EMBL:KJZ21052.1};
GN   ORFNames=TW80_07575 {ECO:0000313|EMBL:KJZ21052.1};
OS   Loktanella sp. S4079.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Loktanella.
OX   NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ21052.1, ECO:0000313|Proteomes:UP000033741};
RN   [1] {ECO:0000313|EMBL:KJZ21052.1, ECO:0000313|Proteomes:UP000033741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4079 {ECO:0000313|EMBL:KJZ21052.1,
RC   ECO:0000313|Proteomes:UP000033741};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ21052.1}.
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DR   EMBL; JXYE01000002; KJZ21052.1; -; Genomic_DNA.
DR   RefSeq; WP_045997093.1; NZ_JXYE01000002.1.
DR   AlphaFoldDB; A0A0F4RQN8; -.
DR   STRING; 579483.TW80_07575; -.
DR   PATRIC; fig|579483.3.peg.1552; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000033741; 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:KJZ21052.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033741}.
FT   DOMAIN          3..57
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          64..444
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          510..588
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   630 AA;  68783 MW;  D6324609F91D5541 CRC64;
     MGYAEVYKGW QDDPEGFWME QAKAIDWDSP PTKALFGDNA PFYEWFADAK VNTCYNAVDR
     HVENGHGEQT AIIYDSPIAH TKREISYVEL RNRVASLAGA LRAKGVEKGD RVIIYMPMIP
     EALEAMLACA RLGAIHSVVF GGFAANELAV RIDDAKPKAI IAASCGMEPG RVVHYKPLLD
     GAIEMAAHKP EFCVIFQREQ EVAELIPGRD YNWHGFQYGV TPAECVPVEG NHPAYILYTS
     GTTGAPKGVV RPTAGHLVAL NWTMKNIYNV DPGDVFWAAS DVGWVVGHSY ICYAPLIHGN
     TTIVFEGKPI GTPDAGTFWR VIQEHNVKSF FTAPTAFRAV KREDPTGEFV KKYDLSCLNA
     IYLAGERADP DTINWTQEKT GKPVYDHWWQ TETGYAIAGN PVGIEPLPVK IGSPTVPMPG
     YDVQILDDGG HPVAAGELGA IAIKLPLPPG TLPTLWNAQD RFEKSYLTTF PGYYETGDAG
     MIDEDGYVYI MARTDDVINV AGHRLSTGAM EEVLANHPDV GECAVIGVTD QLKGQLPMGF
     VCLNKGCTRS HEDITKEVVK SVRDTIGPVA AFKLVAVVDR LPKTRSGKIL RGTMVKIADN
     AEFKMPATID DPAILDEIKA ALRPLGYAGA
//
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