ID A0A1T1HSW4_9PSED Unreviewed; 439 AA.
AC A0A1T1HSW4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=MF4836_22860 {ECO:0000313|EMBL:OOV92945.1};
OS Pseudomonas sp. MF4836.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1960827 {ECO:0000313|EMBL:OOV92945.1, ECO:0000313|Proteomes:UP000190183};
RN [1] {ECO:0000313|Proteomes:UP000190183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF4836 {ECO:0000313|Proteomes:UP000190183};
RA Fagerlund A.;
RT "Genome sequencing of bacteria from food industry.";
RL Submitted (FEB-2017) 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:OOV92945.1}.
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DR EMBL; MVOL01000010; OOV92945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1HSW4; -.
DR STRING; 1960827.MF4836_22860; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000190183; 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; IPR049623; PA_CoA_lig_proteobact_actino.
DR InterPro; IPR011880; PA_CoA_ligase.
DR NCBIfam; TIGR02155; PA_CoA_ligase; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR PANTHER; PTHR43439:SF1; PHENYLACETATE-COENZYME A LIGASE; 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:OOV92945.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 89..296
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 342..438
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 439 AA; 49313 MW; 871A866B7081DB6E CRC64;
MNMPIAKAVL DPVLDPLETA SIDQLRQHQL DRLRWSLNHA YNNVPLYRQR FDELGVHPDD
VRSLDDLAKF PFTTKSDLRD NYPYGMFAVP MQDVVRLHAS SGTTGKPTVV GYTQNDIDTW
ANVVARSIRA GGGRRGDKVH ISYGYGLFTG GLGAHYGAER LGCTVIPMSG GQTEKQVQLI
KDFQPDIIMV TPSYMLNIAD EIERQGIDPQ KLALRLGIFG AEPWTAELRS AIEQRLGITA
LDIYGLSEIM GPGVAMECAE TKDGPTIWED HFYPEIIDPI TGEVLPDGQM GELVFTSLSK
EALPMIRYRT RDLTRLLPGT ARPMRRIDKI TGRSDDMLII RGVNVFPTQV EEQVLKVRQL
CESYEIHLYR NGNLDSVDVH VELKSEHQHL PEEQQKTICS ELSRHIKTNI GISSRIVLQP
AFSIKRSEGK ACHVIDNRK
//
