ID A0A0N1BT27_9PROT Unreviewed; 632 AA.
AC A0A0N1BT27;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Propionate--CoA ligase {ECO:0000313|EMBL:KPF82689.1};
DE EC=6.2.1.17 {ECO:0000313|EMBL:KPF82689.1};
GN Name=prpE {ECO:0000313|EMBL:KPF82689.1};
GN ORFNames=IP70_19670 {ECO:0000313|EMBL:KPF82689.1};
OS alpha proteobacterium AAP38.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF82689.1, ECO:0000313|Proteomes:UP000037884};
RN [1] {ECO:0000313|EMBL:KPF82689.1, ECO:0000313|Proteomes:UP000037884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP38 {ECO:0000313|EMBL:KPF82689.1,
RC ECO:0000313|Proteomes:UP000037884};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF82689.1}.
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DR EMBL; LJHR01000035; KPF82689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1BT27; -.
DR STRING; 1523418.IP70_19670; -.
DR PATRIC; fig|1523418.3.peg.2448; -.
DR OrthoDB; 4471305at2; -.
DR Proteomes; UP000037884; 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:KPF82689.1}.
FT DOMAIN 5..59
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 65..446
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 512..590
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 632 AA; 68575 MW; 015D36C1D8673426 CRC64;
MSGRYQAMHE RSLSDPTGFW ADAARAIDWD VFPTTILDDS DKPFYRWYRG GRLNICHNAL
DRHVAGGRAE QAALIYDSPV TGVKQTLTYA QLLDKVARFA GVLRGLGVGK GDRVIIYMPM
IPEAVVGMLA CARIGAVHSV VFGGFAPHEL ATRINDATPK AILSASCGIE GAKVLAYKPM
LDAAIDQASH KPDHCVIFQR PQALASLIPG RDINWDESAA TAEPAACVAV EATDPLYVLY
TSGTTGQPKG VVRDTGGYAV ALKWTMEHFY GVKPGEVFWA ASDVGWVVGH SYIVYGPLLH
GCTTLVYEGK PVATPDAGAF WRVISEHKVA VQFTAPTAFR AIKREDPNGE LLGQYDMSCL
RALFLAGERS DPDTLNWAET HLKVPVIDHW WQTETGWPVA GNPLGIDLMK VKYGSTAVPL
PGWDIRVLAP DGTEVKRGDI GAIVAKLPLP PGTLPTLWNA RDRFFKSYLA DFPGYYQTSD
AGFIDEDGYI YVMARTDDII NVAGHRLSTG AMEEVLSGHP DVAECAVIGV ADDLKGQLPL
GFVVLKRGVD RPHADIIKEV VKKVRDEIGP VAAFKQALVV ERLPKTRSGK ILRGTMQKIA
DSETWRMPAT IDDPAILGEI GDALKSAGYA KG
//
