ID A0A1H3ZBR2_9BACI Unreviewed; 441 AA.
AC A0A1H3ZBR2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=SAMN05421743_103192 {ECO:0000313|EMBL:SEA21107.1};
OS Thalassobacillus cyri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Thalassobacillus.
OX NCBI_TaxID=571932 {ECO:0000313|EMBL:SEA21107.1, ECO:0000313|Proteomes:UP000198584};
RN [1] {ECO:0000313|EMBL:SEA21107.1, ECO:0000313|Proteomes:UP000198584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM7597 {ECO:0000313|EMBL:SEA21107.1,
RC ECO:0000313|Proteomes:UP000198584};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNQR01000003; SEA21107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3ZBR2; -.
DR STRING; 571932.SAMN05421743_103192; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000198584; 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:SEA21107.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000198584}.
FT DOMAIN 78..285
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 334..434
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 441 AA; 49095 MW; 6632DC484607BB23 CRC64;
MILHGVESAS SEEMKGLQLK RLQETVHRVY ENVPYFKQKF DEMGLVPEDI RSLDDVTKLP
FLEKKALRDN YPFGLFAVDR SELVRIHASS GTSGKPTVVG YTKNDICMWS ELVARAITIG
GGKPGEVLHN AYGYGLFTGG LGLHCGSEEL GMATVPISGG NTERQISLIE DFKPTVICGT
PSYLLNIAEH MEQDGKDPRQ TSLKFGIFGA EPWSEEMRRT LEEKFDIKAC DIYGLSEVLG
PGVAMECHEA QDGLHIAEDH FLAEVIDPDT LEPVPDGEDG ELVFTSLTKE AFPVIRYRTG
DIASLQRGKC KCGRTTVKMS RVKGRIDDML IIRGVNVFPS EIEHYLLSVE GIVPHYQLHV
FKKGSMQHVE LQVEVDEPFF NQIEEDLDHP DVGKLGKHIQ KVMKNNCLIS VEVKVLGPKS
VPRSEGKAVR IVDRTNDTIE V
//
