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Database: UniProt
Entry: E5WN01_9BACI
LinkDB: E5WN01_9BACI
Original site: E5WN01_9BACI 
ID   E5WN01_9BACI            Unreviewed;       435 AA.
AC   E5WN01;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=HMPREF1013_03947 {ECO:0000313|EMBL:EFV75887.1};
OS   Bacillus sp. 2_A_57_CT2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV75887.1, ECO:0000313|Proteomes:UP000003283};
RN   [1] {ECO:0000313|EMBL:EFV75887.1, ECO:0000313|Proteomes:UP000003283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV75887.1,
RC   ECO:0000313|Proteomes:UP000003283};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL   Submitted (DEC-2010) 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:EFV75887.1}.
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DR   EMBL; ACWD01000058; EFV75887.1; -; Genomic_DNA.
DR   RefSeq; WP_009334764.1; NZ_GL635754.1.
DR   AlphaFoldDB; E5WN01; -.
DR   eggNOG; COG1541; Bacteria.
DR   HOGENOM; CLU_035301_1_1_9; -.
DR   UniPathway; UPA00930; -.
DR   Proteomes; UP000003283; 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:EFV75887.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003283}.
FT   DOMAIN          78..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   435 AA;  48695 MW;  F518687749DD5366 CRC64;
     MILHDIETES RDFIEQLQLD RLKQTVERVF NHVPFYRKKF LESNIAPEDV NSLNDIQKLP
     FTVKADLREH YPFGLFAVDK KEIVRLHASS GTSGKPTVVG YTRNDIKMWS NLIARAISIG
     GGEPGQTLHN AYGYGLFTGG LGLHYGSEQL GMATVPVSGG NTDRQIMLIQ DFKPEVICGT
     PSYILNLAEK MEERGMDPAD TSLKYGIFGA EPWSEEMRKT LEAKLGIKAC DIYGLSEVLG
     PGVAMECHES QDGLHIAEDH FYAEVIDPKK MTPLPNGEEG ELVFTSLTKE AFPVIRYRTG
     DIASLSKEKC VCGRTTLRMS RVKGRIDDML NVNGVNVFPS EIERCILQMP ELSPHYHIQV
     YNKGSLKVLE LHAEWSEEFY RDMGEAEHVK KKIKEAVKQN CFITIGLVLH PPKTLPRSDG
     KAVRIVDPAV ENAVT
//
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