ID D5EVC7_PRER2 Unreviewed; 432 AA.
AC D5EVC7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=PRU_0059 {ECO:0000313|EMBL:ADE82735.1};
OS Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Xylanibacter.
OX NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE82735.1, ECO:0000313|Proteomes:UP000000927};
RN [1] {ECO:0000313|EMBL:ADE82735.1, ECO:0000313|Proteomes:UP000000927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG North American Consortium for Rumen Bacteria;
RA Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA Coutinho P.M., Henrissat B., Nelson K.E.;
RT "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT bryantii: insights into their environmental niche.";
RL Microb. Ecol. 60:721-729(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002006; ADE82735.1; -; Genomic_DNA.
DR RefSeq; WP_013064721.1; NC_014033.1.
DR AlphaFoldDB; D5EVC7; -.
DR STRING; 264731.PRU_0059; -.
DR GeneID; 69976694; -.
DR KEGG; pru:PRU_0059; -.
DR eggNOG; COG1541; Bacteria.
DR HOGENOM; CLU_035301_1_1_10; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000000927; 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; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR PANTHER; PTHR43439:SF1; PHENYLACETATE-COENZYME A LIGASE; 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:ADE82735.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000000927}.
FT DOMAIN 78..284
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 334..430
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 432 AA; 48875 MW; 6C400AF12AB2B09E CRC64;
MIWNETMECM DREQLREIQS QRLVKMAEYV YYNTPFYRKK FQEMGLEPGD IKSIDDITKL
PFTNKLDLRD NYPFGLAAVP MSQIVRIHAS SGTTGKPVVV LYTRKDLAMW SEAISRAFTA
YGAGKDDIFQ VAYGYGLFTG GLGAHDGATN IGASVIPISS GNTQKQMTLM HDFGTTILCC
TPSYAMFLGE AMKECPWSRD EFKLKVGVFG AEPWTEKMRK KLEESLGIKA YDIYGLSEIA
GPGVGYECEH QCGTHLNEDL FYPEILDPKT GEPLPEGQFG ELTFTHLTKE GMPLLRYRTH
DLTALHYDKC KCGRTLVRMD RILGRCDDML IIRGVNVFPS QIEDVILKLP EYEPHFLLTV
DRVNNTDTSE LKVEVKEEYF TDDMATMVGL QKKLEGELRS VIGLGFKVKL VEPKGIERSE
GKAKRVIDKR NI
//
