ID A0A0J5FWM0_9GAMM Unreviewed; 443 AA.
AC A0A0J5FWM0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=AB204_04015 {ECO:0000313|EMBL:KMJ46372.1};
OS Xenorhabdus khoisanae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=880157 {ECO:0000313|EMBL:KMJ46372.1, ECO:0000313|Proteomes:UP000036277};
RN [1] {ECO:0000313|EMBL:KMJ46372.1, ECO:0000313|Proteomes:UP000036277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCB {ECO:0000313|EMBL:KMJ46372.1,
RC ECO:0000313|Proteomes:UP000036277};
RA Naidoo S., Featherston J., Gray V.M.;
RT "Draft Whole-Genome Sequence of the Entomopathogenic Bacterium Xenorhabdus
RT khoisanae.";
RL Submitted (JUN-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:KMJ46372.1}.
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DR EMBL; LFCV01000022; KMJ46372.1; -; Genomic_DNA.
DR RefSeq; WP_047962096.1; NZ_LFCV01000022.1.
DR AlphaFoldDB; A0A0J5FWM0; -.
DR STRING; 880157.AB204_04015; -.
DR PATRIC; fig|880157.4.peg.837; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000036277; 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; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR PANTHER; PTHR43439:SF1; PHENYLACETATE-COENZYME A LIGASE; 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:KMJ46372.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 92..298
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 345..440
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 443 AA; 50350 MW; 1576B2E191BC662F CRC64;
MSNNVQHLKK SREQDLDPME FASRDEIQAW QFQQIKWTLN HAYNNVPMYR QKFDAAGIHP
SDFKQLDDII KFPCTTKQDL RDHYPFGAFA VPMEQIVRIH ASSGITGSPT VVGYTQRDID
NWANIIARCL RLAGVCSKDK VHIAYGYGLF TGGLGAHYGA ERLGATVIPM SSGQTEKQAK
LVLDFKPDAI MMTPSYCLTL LDELERKMGG DASKCSLRVG IFGAEPWSDA LRNEIETRMG
IRALDIYGLS EVIGPGVAME SLDDTNGSTI WEDHFYPEII DPDNLNNLAN GETGELILTT
LTKEAMPVIR YRTRDLTRIF PGTTRNMYRL SKIIERSDDM LIIRGVNVFP SQVEEQIMRI
KELSPHYQLE VNRIKNYDKL SVKVELKKSE LLNDQQRYDI CHQLRYHIKS MIGLNTEVSI
VNHGDIPRSE GKAVRVLDNR LHD
//
