ID   D5WZE1_THIK1            Unreviewed;       440 AA.
AC   D5WZE1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   OrderedLocusNames=Tint_3005 {ECO:0000313|EMBL:ADG32339.1};
OS   Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG32339.1};
RN   [1] {ECO:0000313|EMBL:ADG32339.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 {ECO:0000313|EMBL:ADG32339.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA   Heinhorst S., Woyke T.;
RT   "Complete sequence of Thiomonas intermedia K12.";
RL   Submitted (APR-2010) 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; CP002021; ADG32339.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5WZE1; -.
DR   STRING; 75379.Tint_3005; -.
DR   KEGG; tin:Tint_3005; -.
DR   eggNOG; COG1541; Bacteria.
DR   HOGENOM; CLU_035301_1_1_4; -.
DR   BioCyc; TINT75379:TINT_RS15060-MONOMER; -.
DR   UniPathway; UPA00930; -.
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:ADG32339.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT   DOMAIN          94..292
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          339..436
FT                   /note="AMP-dependent ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14535"
SQ   SEQUENCE   440 AA;  49053 MW;  83D9F73E668709DF CRC64;
     MLSPVATAVK PEPIETATRD EIASLQLDRL RWTLHHAYEN VPHYRRAFDA KGVHPDDLHS
     LEDLAKFPFT AKSDLRDNYP FGMFAVPRER IVRVHASSGT TGKPTVVGYT QRDIDTWANL
     VARSIRAAGG KPGDIVHVAY GYGLFTGGMG AHYGAERLGC TVVPMSGGQT EKQVQLIRDF
     QPDIIMVTPS YMQVIIEEFA RQGLDARDCS LRIGIFGAEP WTEAMRREIE SKTSLKAVDI
     YGLSEVMGPG VACECVETQD GPVIWEDHFY PEIIDPITGA PLPDGSEGEL VFTTLTKEGL
     PIIRYRTRDL TRLLPPTARA FRRMGKIVGR SDDMLIVRGV NVFPTQIEEI VIQHDKLSGQ
     YQIHLSRDGH LDKVEVHCEL QPTLGHVSDA ERQQIADWLT HRIKTLVGIS TRVCVLPPDS
     IERTLVGKAR RVIDHRPRGG
//