ID   PAAK_THET2              Reviewed;         445 AA.
AC   Q72K16;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Phenylacetate-coenzyme A ligase;
DE            EC=6.2.1.30;
DE   AltName: Full=Phenylacetyl-CoA ligase;
DE            Short=PA-CoA ligase;
GN   OrderedLocusNames=TT_C0602;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
RN   [2]
RP   FUNCTION AS A LIGASE AND IN PHENYLACETATE CATABOLISM, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND CATALYTIC ACTIVITY.
RX   PubMed=18414813; DOI=10.1007/s00284-008-9147-3;
RA   Erb T.J., Ismail W., Fuchs G.;
RT   "Phenylacetate metabolism in thermophiles: characterization of
RT   phenylacetate-CoA ligase, the initial enzyme of the hybrid pathway in
RT   Thermus thermophilus.";
RL   Curr. Microbiol. 57:27-32(2008).
CC   -!- FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to
CC       phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism.
CC       {ECO:0000269|PubMed:18414813}.
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:0000269|PubMed:18414813};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6 uM for ATP (at 50 degrees Celsius and pH 7.5)
CC         {ECO:0000269|PubMed:18414813};
CC         KM=30 uM for CoA (at 50 degrees Celsius and pH 7.5)
CC         {ECO:0000269|PubMed:18414813};
CC         KM=50 uM for PA (at 50 degrees Celsius and pH 7.5)
CC         {ECO:0000269|PubMed:18414813};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius. The enzyme is heat stable.
CC         {ECO:0000269|PubMed:18414813};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phenylacetyl-CoA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; AE017221; AAS80950.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q72K16; -.
DR   SMR; Q72K16; -.
DR   STRING; 262724.TT_C0602; -.
DR   EnsemblBacteria; AAS80950; AAS80950; TT_C0602.
DR   KEGG; tth:TT_C0602; -.
DR   eggNOG; COG1541; Bacteria.
DR   HOGENOM; CLU_035301_1_1_0; -.
DR   OMA; GVAPHFQ; -.
DR   BRENDA; 6.2.1.30; 2305.
DR   UniPathway; UPA00930; -.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0047475; F:phenylacetate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IDA:UniProtKB.
DR   CDD; cd05913; PaaK; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR028154; AMP-dep_Lig_C.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR011880; PA_CoA_ligase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF14535; AMP-binding_C_2; 1.
DR   PIRSF; PIRSF006444; PaaK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..445
FT                   /note="Phenylacetate-coenzyme A ligase"
FT                   /id="PRO_0000416774"
SQ   SEQUENCE   445 AA;  49599 MW;  B919E41C2901021B CRC64;
     MMYQPELETL PREKLRALQE ERLKRLVAYV YERVPFYRRL LDEAGVDPKG FRGLEDLPRI
     PFTKKTDLRD HYPFGLFAVP REEVARVHAS SGTTGKPTVV GYTKNDLKVF AEVVARSLAA
     AGARPGMMLH NAYGYGLFTG GLGLHGGAEA LGMTVVPVSG GMTERQVMLI QDFRPEVISC
     TPSYAQTLAE EFRKRGVSPE ELSLEYAVLG AEPWTEAIRK QVDEGLGVKS TNIYGLSEII
     GPGVSNECVE ERQGSHIWED HFLPEVVDPD TGEPLPEGKV GVLVFTTLTK EAMPLLRYWT
     GDLTFLTYEA CTCGRTHVRM GPILGRTDDM LIIRGVNVYP TQVEAVLLAI PEVVPHYQIV
     VRREGTLDEA ELKVEVSEPF FREIGQEVLS DEVVEADHRL HALRERIARK IKDNVGVTLK
     VTLLPPGQAP RSEGGKLRRV LDLRK