ID Q8AAN6_BACTN Unreviewed; 435 AA. AC Q8AAN6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 12-OCT-2022, entry version 122. 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=BT_0428 {ECO:0000313|EMBL:AAO75535.1}; OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO75535.1, ECO:0000313|Proteomes:UP000001414}; RN [1] {ECO:0000313|EMBL:AAO75535.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414}; RX PubMed=12663928; DOI=10.1126/science.1080029; RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., RA Hooper L.V., Gordon J.I.; RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."; RL Science 299:2074-2076(2003). RN [2] {ECO:0000313|EMBL:AAO75535.1, ECO:0000313|Proteomes:UP000001414} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414}; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of its two RT dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). RN [3] {ECO:0007829|PDB:4R1L} RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) IN COMPLEX WITH ADP; AMP; COENZYME A RP AND ZINC. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of a Hypothetical Acyl-CoA ligase (BT_0428) from RT Bacteroides thetaiotaomicron VPI-5482 at 2.42 A resolution."; RL Submitted (AUG-2014) to the PDB data bank. RN [4] {ECO:0007829|PDB:4R1M} RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) IN COMPLEX WITH AMP AND ZINC. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of a Hypothetical Acyl-CoA ligase (BT_0428) from RT Bacteroides thetaiotaomicron VPI-5482 at 2.48 A resolution."; RL Submitted (AUG-2014) to the PDB data bank. RN [5] {ECO:0007829|PDB:4RVN} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH AMP; COENZYME A AND RP ZINC. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of a Putative Acyl-CoA ligase (BT_0428) from Bacteroides RT thetaiotaomicron VPI-5482 at 2.20 A resolution."; RL Submitted (NOV-2014) to the PDB data bank. RN [6] {ECO:0007829|PDB:4RVO} RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH ADP AND ZINC. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of a Putative Acyl-CoA ligase (BT_0428) from Bacteroides RT thetaiotaomicron VPI-5482 at 2.41 A resolution."; RL Submitted (NOV-2014) to the PDB data bank. 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; AE015928; AAO75535.1; -; Genomic_DNA. DR RefSeq; NP_809341.1; NC_004663.1. DR RefSeq; WP_008760705.1; NC_004663.1. DR PDB; 4R1L; X-ray; 2.42 A; A/B/C/D=1-435. DR PDB; 4R1M; X-ray; 2.48 A; A/B/C/D=1-435. DR PDB; 4RVN; X-ray; 2.20 A; A/B/C/D=1-435. DR PDB; 4RVO; X-ray; 2.41 A; A/B/C/D=1-435. DR PDBsum; 4R1L; -. DR PDBsum; 4R1M; -. DR PDBsum; 4RVN; -. DR PDBsum; 4RVO; -. DR SMR; Q8AAN6; -. DR STRING; 226186.BT_0428; -. DR PaxDb; Q8AAN6; -. DR PRIDE; Q8AAN6; -. DR DNASU; 1071713; -. DR EnsemblBacteria; AAO75535; AAO75535; BT_0428. DR GeneID; 60926386; -. DR KEGG; bth:BT_0428; -. DR PATRIC; fig|226186.12.peg.427; -. DR eggNOG; COG1541; Bacteria. DR HOGENOM; CLU_035301_1_1_10; -. DR InParanoid; Q8AAN6; -. DR OMA; IHCTPSY; -. DR UniPathway; UPA00930; -. DR EvolutionaryTrace; Q8AAN6; -. DR Proteomes; UP000001414; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; -; 1. DR InterPro; IPR045851; AMP-bd_C_sf. DR InterPro; IPR028154; AMP-dep_Lig_C. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR InterPro; IPR042099; ANL_N_sf. DR InterPro; IPR011880; PA_CoA_ligase. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF14535; AMP-binding_C_2; 1. DR PIRSF; PIRSF006444; PaaK; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M}; KW Ligase {ECO:0000256|PIRNR:PIRNR006444, ECO:0000313|EMBL:AAO75535.1}; KW Metal-binding {ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444, ECO:0007829|PDB:4R1L}; KW Reference proteome {ECO:0000313|Proteomes:UP000001414}; KW Zinc {ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M}. FT DOMAIN 93..287 FT /note="AMP-binding" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 337..432 FT /note="AMP-binding_C_2" FT /evidence="ECO:0000259|Pfam:PF14535" FT BINDING 94 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4RVO" FT BINDING 164 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT BINDING 166 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT BINDING 187 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT BINDING 190 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT BINDING 214 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 214 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 215 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 215 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 216 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4RVO" FT BINDING 216 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1M, ECO:0007829|PDB:4RVN" FT BINDING 235 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 235 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 236 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 236 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 240 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 240 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 251 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 304 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 304 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 313 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 315 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 328 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 328 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1M, ECO:0007829|PDB:4RVN" FT BINDING 336 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT BINDING 337 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 339 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 339 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 407 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT BINDING 424 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 424 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4R1M, ECO:0007829|PDB:4RVN" SQ SEQUENCE 435 AA; 49380 MW; 50F97E048724D7A2 CRC64; MSTQYWEEEI EIMSREKLQE LQLQRLKKTI NIAANSPYYK EVFSKNGITG DSIQSLDDIR KIPFTTKSDM RANYPFGLVA GDMKRDGVRI HSSSGTTGNP TVIVHSQHDL DSWANLVARC LYMVGIRKTD VFQNSSGYGM FTGGLGFQYG AERLGCLTVP AAAGNSKRQI KFISDFKTTA LHAIPSYAIR LAEVFQEEGI DPRETTLKTL VIGAEPHTDE QRRKIERMLN VKAYNSFGMT EMNGPGVAFE CQEQNGMHFW EDCYLVEIID PETGEPVPEG EIGELVLTTL DREMMPLIRY RTRDLTRILP GKCPCGRTHL RIDRIKGRSD DMFIIKGVNI FPMQVEKILV QFPELGSNYL ITLETVNNQD EMIVEVELSD LSTDNYIELE KIRRDIIRQL KDEILVTPKV KLVKKGSLPQ SEGKAVRVKD LRDNK //