ID A0A1I7LG62_9BRAD Unreviewed; 443 AA.
AC A0A1I7LG62;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05192541_11452 {ECO:0000313|EMBL:SFV08671.1};
OS Bradyrhizobium arachidis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=858423 {ECO:0000313|EMBL:SFV08671.1, ECO:0000313|Proteomes:UP000199591};
RN [1] {ECO:0000313|EMBL:SFV08671.1, ECO:0000313|Proteomes:UP000199591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26795 {ECO:0000313|EMBL:SFV08671.1,
RC ECO:0000313|Proteomes:UP000199591};
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; FPBQ01000014; SFV08671.1; -; Genomic_DNA.
DR RefSeq; WP_027558588.1; NZ_FPBQ01000014.1.
DR AlphaFoldDB; A0A1I7LG62; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000199591; 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:SFV08671.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 94..299
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 346..440
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 443 AA; 49599 MW; F56885D8AA514E32 CRC64;
MALTRLKEGG NSYSAEMDAH ERASRDEIVA LQKQRLAWSL KHAYDNVAHY RKAFDKAGVH
PSDFRELSDL AKFPFTVKTD LRDNYPFNMF AVPREKLVRV HASSGTTGKP IVVGYTQRDI
DTWSEVMARS IRAAGGRTGM IIHNAYGYGL FTGGLGVHYG AEKLGCTVVP ISGGMTERQV
QLINDFRPDI ITVTPSYMLA ILDEFKRQKL DPRQCSLKVG IFGAEPWTNA MRGEIEDAFD
MDATDIYGLS EVIGPGVAQE CIETKDGLHI WEDHFYPEVI DPETGAVLPD GERGELVFTS
LTKEAFPVIR YRTRDLTRLL PGTARPGMRR MEKVTGRSDD MIILRGVNLF PTQIEEVLLA
TDWCGGHFIL ELTREGRMDE LTIIAEARPE SWDGRGLVDH ADRVSTHIKN TIGISSRVQV
VAPATLERSL GKAKRLYDKR PKD
//