ID A0A143XWR4_9FIRM Unreviewed; 433 AA.
AC A0A143XWR4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=NDGK_02411 {ECO:0000313|EMBL:CVI72016.1};
OS Clostridiales bacterium CHKCI001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1780378 {ECO:0000313|EMBL:CVI72016.1, ECO:0000313|Proteomes:UP000198774};
RN [1] {ECO:0000313|EMBL:CVI72016.1, ECO:0000313|Proteomes:UP000198774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC1 {ECO:0000313|EMBL:CVI72016.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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; FCNS01000037; CVI72016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143XWR4; -.
DR STRING; 1780378.NDGK_02411; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000198774; 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; 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:CVI72016.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000198774}.
FT DOMAIN 60..286
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 335..430
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 433 AA; 48752 MW; AA53F33D596C0C5E CRC64;
MENYYQPEIE CASREQIQAW QDERLVKQVK HVYEHVPYYR KKMEEKGVVP EDIRSTADLH
KLPFLTKDDL RQAYPYGLLA TPLEDVVRIQ STSGTTGRRV VAFYTQHDID LWDECCARAI
MAAGGTKKDV VHVCYGYGLF TGGPGLNGGS HKVGSMTLPM SSGNTERQIQ FMCDLGSTIL
CCTPSYAAYL AESINERGLR DKIKLKAGIF GAEAWTEEMR RDIEKSLGIK AYDIYGLTEI
SGPGVSFECS EQRGMHINED HFIAEIIDPV TGEVLPEGEK GELVFTSITK EAFPLLRYRT
RDICVLSREK CSCGRTHVRM SKPMGRSDDM MIIKGVNVFP SQIETVLLNK GYPANYQIIV
NRVNNSDTLE VQVEMTPEMF SDSVTKIAAQ ERELVDALKA MLGIYARVRL VEPKTIARSE
GKAVRVIDKR NLY
//
