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Database: UniProt
Entry: A0A0W7X5Z3_9ACTN
LinkDB: A0A0W7X5Z3_9ACTN
Original site: A0A0W7X5Z3_9ACTN 
ID   A0A0W7X5Z3_9ACTN        Unreviewed;       431 AA.
AC   A0A0W7X5Z3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=AT728_24995 {ECO:0000313|EMBL:KUF18232.1};
OS   Streptomyces silvensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF18232.1, ECO:0000313|Proteomes:UP000054804};
RN   [1] {ECO:0000313|EMBL:KUF18232.1, ECO:0000313|Proteomes:UP000054804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF18232.1,
RC   ECO:0000313|Proteomes:UP000054804};
RA   Johnston C.W., Li Y., Magarvey N.A.;
RT   "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT   novel hormone antagonists.";
RL   Submitted (DEC-2015) 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}.
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:KUF18232.1}.
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DR   EMBL; LOCL01000031; KUF18232.1; -; Genomic_DNA.
DR   RefSeq; WP_058847604.1; NZ_LOCL01000031.1.
DR   AlphaFoldDB; A0A0W7X5Z3; -.
DR   STRING; 1765722.AT728_24995; -.
DR   OrthoDB; 580775at2; -.
DR   UniPathway; UPA00930; -.
DR   Proteomes; UP000054804; 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:KUF18232.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054804}.
FT   DOMAIN          94..290
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          336..429
FT                   /note="AMP-dependent ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14535"
SQ   SEQUENCE   431 AA;  47728 MW;  B1E8CD5D9DE04544 CRC64;
     MARTPALLDA AERLGRAELE ALQLERLQDT LLHAYENVPF YRAAFDAAGL GPDDCHTLAD
     LGRFPFTTKA DLRANYPFGM FAVEQSELRR LHASSGTTGR PTVVGYTEQD LNMWADVVAR
     SIRAAGGRPG HKVHVAYGYG LFTGGLGAHY GAERLGCTVI PASGGMTARQ VQLILDFRPE
     IIMVTPSYML TLLEEFERQG IDPRTTSLQV GIFGAEPWTE AMRTEIEERF AIDAVDIYGL
     SEVIGPGVAQ ECVETKDGLH IWEDHFYPEV VDPITGRVLP DGEHGELVFT SLTKEALPVI
     RYRTRDLTRL LPGTARAFRR MEKITGRSDD MVILRGVNLF PTQIEEIVLG TPGLAPHFQL
     RLTREGRLDA LTVRVEARPD TPRGRRETAA REIESAVKDG IGVSVAVEVV DPESIERSVG
     KIRRIVDLRE K
//
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