ID A0A158IBY2_9BURK Unreviewed; 434 AA.
AC A0A158IBY2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=AWB64_05923 {ECO:0000313|EMBL:SAL53977.1};
OS Caballeronia sordidicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL53977.1, ECO:0000313|Proteomes:UP000054893};
RN [1] {ECO:0000313|EMBL:SAL53977.1, ECO:0000313|Proteomes:UP000054893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL53977.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FCOC02000033; SAL53977.1; -; Genomic_DNA.
DR RefSeq; WP_060858883.1; NZ_FCOC02000033.1.
DR AlphaFoldDB; A0A158IBY2; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000054893; 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:SAL53977.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 82..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; 47815 MW; E2B83C3699ADB867 CRC64;
MTAPLPLDPI ETASRDELTA LQLERLKWSI AHAYENSPVY RRKFDEAGVH PDDVKSLADI
ARFPFTTKKD LRDNYPYGMF AVPHDQISRI HASSGTTGKP TVVGYTAKDI DTWSDLVARS
IRAAGARRGD KVHVSYGYGL FTGGLGAHYG AERAGLTVIP FGGGQTEKQV QLIQDFRPDI
IMVTPSYMLS IADELERQGV HPADCSLRIG IFGAEPWTND MRAAIEKRMG IDAVDIYGLS
EVMGPGVASE CVETKDGPTI WEDHFYPEII DPDTGEVLPD GELGELVFTS LTKEALPIIR
YRTRDLTRLL PGTARTMRRM EKITGRSDDM MIVRGVNVFP TQIEELLLRQ HALAPHYQIV
LTKEGPLDVL TLNIEPCPET APDAVLLNQA SAALACDIKA LIGVSAVIRL LDVNGIERSV
GKARRVIDRR NAVT
//
