ID Q8AAN6_BACTN Unreviewed; 435 AA. AC Q8AAN6; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 16-JAN-2019, entry version 106. 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 / OS NCTC 10582 / E50 / VPI-5482). 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 / NCTC 10582 / E50 / VPI-5482 RC {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., RA Chiang H.C., 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 / NCTC 10582 / E50 / VPI-5482 RC {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 RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). RN [3] {ECO:0000213|PDB:4R1L} RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) IN COMPLEX WITH ADP; AMP; RP COENZYME A 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:0000213|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:0000213|PDB:4RVN} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH AMP; COENZYME A RP AND ZINC. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of a Putative Acyl-CoA ligase (BT_0428) from RT Bacteroides thetaiotaomicron VPI-5482 at 2.20 A resolution."; RL Submitted (NOV-2014) to the PDB data bank. RN [6] {ECO:0000213|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 RT Bacteroides 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 ProteinModelPortal; Q8AAN6; -. DR SMR; Q8AAN6; -. DR STRING; 226186.BT_0428; -. DR PaxDb; Q8AAN6; -. DR PRIDE; Q8AAN6; -. DR EnsemblBacteria; AAO75535; AAO75535; BT_0428. DR GeneID; 1071713; -. DR GeneID; 31617413; -. DR KEGG; bth:BT_0428; -. DR PATRIC; fig|226186.12.peg.427; -. DR eggNOG; ENOG4105DZS; Bacteria. DR eggNOG; COG1541; LUCA. DR InParanoid; Q8AAN6; -. DR KO; K01912; -. DR OMA; YDSYGLS; -. 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 InterPro; IPR028154; AMP-dep_Lig_C. DR InterPro; IPR000873; AMP-dep_Synth/Lig. 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:0000213|PDB:4R1L, ECO:0000213|PDB:4R1M, KW ECO:0000213|PDB:4RVN, ECO:0000213|PDB:4RVO}; KW Complete proteome {ECO:0000313|Proteomes:UP000001414}; KW Ligase {ECO:0000256|PIRNR:PIRNR006444, ECO:0000313|EMBL:AAO75535.1}; KW Metal-binding {ECO:0000213|PDB:4R1L, ECO:0000213|PDB:4R1M, KW ECO:0000213|PDB:4RVN, ECO:0000213|PDB:4RVO}; KW Nucleotide-binding {ECO:0000213|PDB:4R1L, ECO:0000213|PDB:4R1M, KW ECO:0000213|PDB:4RVN, ECO:0000256|PIRNR:PIRNR006444}; KW Reference proteome {ECO:0000313|Proteomes:UP000001414}; KW Zinc {ECO:0000213|PDB:4R1L, ECO:0000213|PDB:4R1M, KW ECO:0000213|PDB:4RVN, ECO:0000213|PDB:4RVO}. FT DOMAIN 93 287 AMP-binding. {ECO:0000259|Pfam:PF00501}. FT DOMAIN 337 432 AMP-binding_C_2. {ECO:0000259|Pfam: FT PF14535}. FT NP_BIND 214 216 ADP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVO}. FT NP_BIND 214 216 AMP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4R1M, ECO:0000213|PDB: FT 4RVN}. FT NP_BIND 235 236 ADP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVO}. FT NP_BIND 235 236 AMP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4R1M, ECO:0000213|PDB: FT 4RVN}. FT NP_BIND 337 339 ADP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVO}. FT REGION 164 166 Coenzyme A binding. {ECO:0000213|PDB: FT 4R1L, ECO:0000213|PDB:4RVN}. FT REGION 187 190 Coenzyme A binding. {ECO:0000213|PDB: FT 4R1L, ECO:0000213|PDB:4RVN}. FT METAL 251 251 Zinc. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4R1M, ECO:0000213|PDB: FT 4RVN}. FT METAL 258 258 Zinc; via tele nitrogen. FT {ECO:0000213|PDB:4R1L, ECO:0000213|PDB: FT 4R1M, ECO:0000213|PDB:4RVN}. FT METAL 313 313 Zinc. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4R1M, ECO:0000213|PDB: FT 4RVN}. FT METAL 315 315 Zinc. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4R1M, ECO:0000213|PDB: FT 4RVN}. FT BINDING 94 94 ADP. {ECO:0000213|PDB:4RVO}. FT BINDING 240 240 ADP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVO}. FT BINDING 240 240 AMP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4R1M, ECO:0000213|PDB: FT 4RVN}. FT BINDING 304 304 ADP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVO}. FT BINDING 304 304 AMP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4R1M, ECO:0000213|PDB: FT 4RVN}. FT BINDING 328 328 ADP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVO}. FT BINDING 328 328 AMP. {ECO:0000213|PDB:4R1M, FT ECO:0000213|PDB:4RVN}. FT BINDING 336 336 Coenzyme A. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVN}. FT BINDING 339 339 AMP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4R1M, ECO:0000213|PDB: FT 4RVN}. FT BINDING 407 407 Coenzyme A. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVN}. FT BINDING 424 424 ADP. {ECO:0000213|PDB:4R1L, FT ECO:0000213|PDB:4RVO}. FT BINDING 424 424 AMP. {ECO:0000213|PDB:4R1M, FT ECO:0000213|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 //