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
//