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Database: UniProt
Entry: A0A0C1JEJ5_9RHOB
LinkDB: A0A0C1JEJ5_9RHOB
Original site: A0A0C1JEJ5_9RHOB 
ID   A0A0C1JEJ5_9RHOB        Unreviewed;       633 AA.
AC   A0A0C1JEJ5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:KIC45857.1};
DE            EC=6.2.1.17 {ECO:0000313|EMBL:KIC45857.1};
GN   Name=prpE {ECO:0000313|EMBL:KIC45857.1};
GN   ORFNames=RA28_09270 {ECO:0000313|EMBL:KIC45857.1};
OS   Ruegeria sp. ANG-S4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC45857.1, ECO:0000313|Proteomes:UP000031326};
RN   [1] {ECO:0000313|Proteomes:UP000031326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(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:KIC45857.1}.
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DR   EMBL; JWLK01000002; KIC45857.1; -; Genomic_DNA.
DR   RefSeq; WP_039527099.1; NZ_JWLK01000002.1.
DR   AlphaFoldDB; A0A0C1JEJ5; -.
DR   STRING; 1577904.RA28_09270; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000031326; 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:KIC45857.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031326}.
FT   DOMAIN          3..57
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          64..448
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          514..592
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   633 AA;  68649 MW;  9FF6B6C4223DB4B6 CRC64;
     MSYADAYASW QADPEAFWGK AAEQIDWFKP AEKVFDPEMG VYGRWFAGAT CNTCWNCVDR
     HVEAGNGERT ALIYDSPVTD TVQAFSFSEL QAEVGALASV MRAYGVGKGD RVVIYMPMVP
     QAVFAMLACA RLGAIHSVVF GGFAPHELAT RINDAAPKMI ISASCGIEPG RIVHYKPLLD
     AAIAEAATKP DHCLILQRDM ERADLIPGRD LDYAELVSQA KAAGETTECV PVAATDPLYI
     LYTSGTTGQP KGVVRDNGGH MVALKWTMEH HYGMNPGEVF WAASDVGWVV GHSYICYGPL
     LHGCATVVYE GKPVGTPDAG AFWRVIQDHQ VAALFTAPTA FRAIKKEDPR GLLIEQYNLS
     KFRTQFLAGE RSDPATIQWA EEKLKRPVID HWWQTETGWA MSGNPVGLGQ LPVKYGSPGK
     PMPGYDIRVL DDEGHEVEPG TLGNIVCKLP LPPSGFPTLW NAPERFLTSY MNEFPGFYAT
     SDAGIIDEDG YVFIMARTDD IINVAGHRLS TGAMEEVIGA HPDIAECAVV GAADAMKGQM
     PLGFYVTNDG ANRDAAELEK ELVALMREQI GAVAAFKTAI PVKRLPKTRS GKVLRGTMQK
     IADSAAFKMP AAIDDPAILD EISDALKGRG LLS
//
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