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Database: UniProt
Entry: A0A2A5GFX2_9GAMM
LinkDB: A0A2A5GFX2_9GAMM
Original site: A0A2A5GFX2_9GAMM 
ID   A0A2A5GFX2_9GAMM        Unreviewed;       631 AA.
AC   A0A2A5GFX2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Propionyl-CoA synthetase {ECO:0000313|EMBL:PCJ91415.1};
DE            EC=6.2.1.17 {ECO:0000313|EMBL:PCJ91415.1};
GN   Name=prpE {ECO:0000313|EMBL:PCJ91415.1};
GN   Synonyms=yahU {ECO:0000313|EMBL:PCJ91415.1};
GN   ORFNames=COA46_08205 {ECO:0000313|EMBL:PCJ91415.1};
OS   Porticoccaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae.
OX   NCBI_TaxID=2026782 {ECO:0000313|EMBL:PCJ91415.1, ECO:0000313|Proteomes:UP000230152};
RN   [1] {ECO:0000313|Proteomes:UP000230152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PCJ91415.1}.
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DR   EMBL; NVXH01000008; PCJ91415.1; -; Genomic_DNA.
DR   Proteomes; UP000230152; Unassembled WGS sequence.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
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   InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
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.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:PCJ91415.1}.
FT   DOMAIN          335..378
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
SQ   SEQUENCE   631 AA;  70005 MW;  947EDF9AF64AF784 CRC64;
     MNEQHSYTLQ YDQFLNDPEA FWHEQASLIA WYKKPQTILS KDDNNYFRWY EDGELNTSYL
     CLDYHIEQGR GEQVALIYDS PVTDTKTSFS YKELRDKVAI FAGGLKDLGV SKGDRVVLYM
     SMVPEAVIAM LACARIGAVH SVVFGGFAPE ELAIRIDDAQ PKVIVTTSCG IEVGKVIPYK
     PLVDEAIALS HHKPTKTVVL QRPECHADMX PGQDVDWEXL NSLASPXEPV XVKGTDPLYI
     LYTSGTTGKP KGVVRDNGGH AVAMRYSMET VYDVQPGDVY WAASDVGWVV GHSYIVYAPL
     LTGCTTILYE GKPVRTPDAN AFWRVCEEYG VKXLFTAPTA FRAIRKEDPE ASGLVNYDLS
     KLERIYLAGE RLDPTTYEWL LXKTGLPIID HWWQTETAWA ISGNPIGLGA LPTKAGSATV
     PMPGYNIDIL DDHGDHVAPG EPGNITIKLP LPPGTLTTIW GDHHRFEKSY LSTYPGYYLT
     GDEGYLDKDN YLFVMGRIDD VINVAGHRLS TGKMEEIVSS HDAIAECAVI GVEDSLKGQL
     PMGLVVLKDG VSIEAETLSQ ELRQMMRRKI GAISCYNQTH IIQRLPKTRS GKILRKTLRQ
     VVDGKPYTVP STIDDPEILD EIKAVVVGSR C
//
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