ID A0A1Y3TSD3_9FIRM Unreviewed; 436 AA.
AC A0A1Y3TSD3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B5G27_01945 {ECO:0000313|EMBL:OUN35940.1};
OS Lachnoclostridium sp. An76.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965654 {ECO:0000313|EMBL:OUN35940.1, ECO:0000313|Proteomes:UP000199802};
RN [1] {ECO:0000313|Proteomes:UP000199802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000199802};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUN35940.1}.
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DR EMBL; NFHL01000001; OUN35940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3TSD3; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000199802; 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:OUN35940.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000199802}.
FT DOMAIN 79..286
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 336..432
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 436 AA; 48736 MW; 53443D108F61D697 CRC64;
MIWAKEETLP RDEIEAIQFA KLKGTVRYIY DRVKPYREKM DAAGIKPEDI RSLDDLKKLP
FTYKADFRDN YPDGLFAVDK KEIVRYHASS GTTGKPTVVG YTRNDLDMWL NNVARIACMG
GATADDVAQI SFGYGTFTGA LGLHGGLEKI GASVIPMSSG NTNKQIMFLQ DMGVTLLVAT
PSYALHLGEE IRKRGIDPAK DLKLHIGLFG GEGMTEPMRD EMHKVWGDQF ICTQNYGMSE
LCGPGVAGEC TELCGMHVNE DWFIPEVIDP ETEEVLPPGE LGELVVTCLG KEALPLVRYR
TGDLTRLMYE PCRCGRTTCR IENISGRADD MLVIRGVNVF PTQIEEVLLK IEEIGPHYEI
LVERKNRLDV MTITVELIDD RLLDSYGKLS ELEARIQRAL KAQLGLATQI RLVAPNSLKR
FEGKAKRVTD LRKDGL
//
