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Database: UniProt
Entry: Q5SJP2_THET8
LinkDB: Q5SJP2_THET8
Original site: Q5SJP2_THET8 
ID   Q5SJP2_THET8            Unreviewed;       448 AA.
AC   Q5SJP2;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=TTHA0966 {ECO:0000313|EMBL:BAD70789.1};
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD70789.1, ECO:0000313|Proteomes:UP000000532};
RN   [1] {ECO:0000313|EMBL:BAD70789.1, ECO:0000313|Proteomes:UP000000532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) 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; AP008226; BAD70789.1; -; Genomic_DNA.
DR   RefSeq; YP_144232.1; NC_006461.1.
DR   AlphaFoldDB; Q5SJP2; -.
DR   DNASU; 3168870; -.
DR   EnsemblBacteria; BAD70789; BAD70789; BAD70789.
DR   KEGG; ttj:TTHA0966; -.
DR   PATRIC; fig|300852.9.peg.948; -.
DR   eggNOG; COG1541; Bacteria.
DR   HOGENOM; CLU_035301_1_1_0; -.
DR   PhylomeDB; Q5SJP2; -.
DR   UniPathway; UPA00930; -.
DR   Proteomes; UP000000532; Chromosome.
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; IPR011880; PA_CoA_ligase.
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:BAD70789.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000532}.
FT   DOMAIN          41..288
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          338..447
FT                   /note="AMP-dependent ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14535"
SQ   SEQUENCE   448 AA;  50045 MW;  1D1102F6A9D81501 CRC64;
     MMGMMYQPEL ETLPREKLRA LQEERLKRLV VYVYERVPFY RRLLDEAGVD PKGFRGLEDL
     PRIPFTKKTD LRDHYPFGLF AVPREEVARI HASSGTTGKP TVVGYTKNDL KVFAEVVARS
     LAAAGARPGM MLHNAYGYGL FTGGLGLHGG AEALGMTVVP VSGGMTERQV MLIQDFRPEV
     ISCTPSYAQT LAEEFRKRGV SPEELSLEYA VLGAEPWTEA IRKQVDEGLG VKSTNIYGLS
     EIIGPGVSNE CVEERQGSHI WEDHFLPEVV DPDTGEPLPE GKVGVLVFTT LTKEAMPLLR
     YWTGDLTFLT YEACTCGRTH VRMGPILGRT DDMLIIRGVN VYPTQVEAVL LAIPEVEPYY
     QIVVRREGTL DEAELKVEVS EPFFREIGRE VLSDEVVEAD HRLHALRERI ARKIKDNVGV
     TLKVTLLPPG QAPRSEGGKL RRVLDLRK
//
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