ID A0A0J1CHB7_9BURK Unreviewed; 434 AA.
AC A0A0J1CHB7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phenylacetate-coenzyme A ligase {ECO:0000256|PIRNR:PIRNR006444};
DE EC=6.2.1.30 {ECO:0000256|PIRNR:PIRNR006444};
DE AltName: Full=Phenylacetyl-CoA ligase {ECO:0000256|PIRNR:PIRNR006444};
GN ORFNames=EOS_43115 {ECO:0000313|EMBL:KLU20085.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU20085.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU20085.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
CC -!- FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to
CC phenylacetyl-CoA (PA-CoA). {ECO:0000256|PIRNR:PIRNR006444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylacetate + ATP + CoA = AMP + diphosphate +
CC phenylacetyl-CoA; Xref=Rhea:RHEA:20956, ChEBI:CHEBI:18401,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57390, ChEBI:CHEBI:456215; EC=6.2.1.30;
CC Evidence={ECO:0000256|PIRNR:PIRNR006444};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC {ECO:0000256|PIRNR:PIRNR006444}.
CC -!- SIMILARITY: Belongs to the phenylacetyl-CoA ligase family.
CC {ECO:0000256|PIRNR:PIRNR006444}.
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:KLU20085.1}.
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DR EMBL; AEJF01000377; KLU20085.1; -; Genomic_DNA.
DR RefSeq; WP_047898367.1; NZ_AEJF01000377.1.
DR AlphaFoldDB; A0A0J1CHB7; -.
DR PATRIC; fig|908627.4.peg.9692; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000035963; Unassembled WGS sequence.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0047475; F:phenylacetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0010124; P:phenylacetate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05913; PaaK; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR028154; AMP-dep_Lig_C.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR049623; PA_CoA_lig_proteobact_actino.
DR InterPro; IPR011880; PA_CoA_ligase.
DR NCBIfam; TIGR02155; PA_CoA_ligase; 1.
DR PANTHER; PTHR43845; BLR5969 PROTEIN; 1.
DR PANTHER; PTHR43845:SF1; BLR5969 PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF14535; AMP-binding_C_2; 1.
DR PIRSF; PIRSF006444; PaaK; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|PIRNR:PIRNR006444, ECO:0000313|EMBL:KLU20085.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 90..289
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 335..430
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 434 AA; 47817 MW; D7F33FA4EB91F60D CRC64;
MSTALSLDPI ETASRDELTA LQLERLKWSL AHAYENSPVY RRKFDEAGVH PDDVKTLADL
ARFPFTTKQD LRDNYPYGMF AVPHERISRI HASSGTTGKP TVVGYTAKDI DTWANLVARS
IRAAGARRGD KVHVSYGYGL FTGGLGAHYG AERAGLTVIP FGGGQTEKQV QLIQDFRPDI
IMVTPSYMLS IADELERQGV HPADCSLRIG IFGAEPWTND MRAAIEKRMG IDAVDIYGLS
EVMGPGVASE CVETKDGPTI WEDHFYPEII DPDTGEVLPD GELGELVFTS LTKEALPIVR
YRTRDLTRLL PGSARTMRRM EKITGRSDDM MIVRGVNVFP TQIEELLLKQ HAFAPHYQIV
LTKEGPLDVL TLNVEPCPET APDTNVLDQA KAALAYDIKA LIGVSAVVQV LGVNGIERSV
GKARRVIDRR KVAS
//
