ID A0A2C6C3S3_9BACT Unreviewed; 427 AA.
AC A0A2C6C3S3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=CEQ90_02500 {ECO:0000313|EMBL:PHI21289.1};
OS Lewinellaceae bacterium SD302.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae.
OX NCBI_TaxID=2014804 {ECO:0000313|EMBL:PHI21289.1, ECO:0000313|Proteomes:UP000223945};
RN [1] {ECO:0000313|EMBL:PHI21289.1, ECO:0000313|Proteomes:UP000223945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD302 {ECO:0000313|EMBL:PHI21289.1,
RC ECO:0000313|Proteomes:UP000223945};
RA Wang K.;
RT "The draft genome sequence of Lewinellaceae bacterium SD302.";
RL Submitted (JUL-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:PHI21289.1}.
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DR EMBL; PDLQ01000003; PHI21289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6C3S3; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000223945; 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:PHI21289.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000223945}.
FT DOMAIN 80..285
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 334..427
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 427 AA; 47304 MW; AC246DA27DEACD38 CRC64;
MYNPSIENLP LDQLRALQNK RLVTLVNRVY KNVPFYQNQF DNIGLHPSDI QSVDDLHKIP
FTQKSDLRDH YPYGLFAKPM DKILRIHASS GTTGKPTVVG YTKNDLDVFD EVVARSLYCA
GARPGMKLHN AYGYGLFTGG LGMHGGATKL GMAVIPVSGG MTERQLTILQ DFRPEVICCT
PSYAQTLAQA FAAKGIDTAD LSARYAILGA EPWTEAIRKE VETGLRVKAT NIYGLSEIIG
PGVSQEDVDE RGSGSYIWED HFYPEVVDKD SGKVLPYGEE GVLVFTTLTK EALPILRYRT
NDICSINYDA NARRTHIKMS SIKGRSDDML IIRGVNLFYT QVEEVINDLA SLSANYRLIV
DKKRSMDSVT VEVELVPGAS VDHSAIAAEL KHKIKNSIGI SMDIELKEPM TIPRSQGGKL
SRIVDLR
//
