ID Q8AAN6_BACTN Unreviewed; 435 AA. AC Q8AAN6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 19-JAN-2022, entry version 120. 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=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 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 BioCyc; BTHE:G13PU-5331-MONOMER; -. 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 NP_BIND 214..216 FT /note="ADP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT NP_BIND 214..216 FT /note="AMP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT NP_BIND 235..236 FT /note="ADP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT NP_BIND 235..236 FT /note="AMP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT NP_BIND 337..339 FT /note="ADP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT REGION 164..166 FT /note="Coenzyme A binding" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT REGION 187..190 FT /note="Coenzyme A binding" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT METAL 251 FT /note="Zinc" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT METAL 258 FT /note="Zinc; via tele nitrogen" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT METAL 313 FT /note="Zinc" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT METAL 315 FT /note="Zinc" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 94 FT /note="ADP" FT /evidence="ECO:0007829|PDB:4RVO" FT BINDING 240 FT /note="ADP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 240 FT /note="AMP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 304 FT /note="ADP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 304 FT /note="AMP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 328 FT /note="ADP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 328 FT /note="AMP" FT /evidence="ECO:0007829|PDB:4R1M, ECO:0007829|PDB:4RVN" FT BINDING 336 FT /note="Coenzyme A" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT BINDING 339 FT /note="AMP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4R1M" FT BINDING 407 FT /note="Coenzyme A" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVN" FT BINDING 424 FT /note="ADP" FT /evidence="ECO:0007829|PDB:4R1L, ECO:0007829|PDB:4RVO" FT BINDING 424 FT /note="AMP" 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 //