ID A0A1M7Q9P9_9BURK Unreviewed; 436 AA.
AC A0A1M7Q9P9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05192549_106385 {ECO:0000313|EMBL:SHN27192.1};
OS Duganella sacchari.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=551987 {ECO:0000313|EMBL:SHN27192.1, ECO:0000313|Proteomes:UP000184339};
RN [1] {ECO:0000313|EMBL:SHN27192.1, ECO:0000313|Proteomes:UP000184339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sac-22 {ECO:0000313|EMBL:SHN27192.1,
RC ECO:0000313|Proteomes:UP000184339};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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; FRCX01000006; SHN27192.1; -; Genomic_DNA.
DR RefSeq; WP_072786106.1; NZ_FRCX01000006.1.
DR AlphaFoldDB; A0A1M7Q9P9; -.
DR STRING; 551987.SAMN05192549_106385; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000184339; 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; 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:SHN27192.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 88..293
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 339..433
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 436 AA; 48431 MW; E498A1B8E2A63DBF CRC64;
MVQRTPDPAD LEPIERASRD ELQALQLQRM QWTLKHAYEN VPHYRAAFDQ AGVHPDDLRT
LADLAKFPFT GKKDLRDNYP FGLFAVPQDR VVRVHASSGT TGKPTVVGYT QNDIDTWAHV
VARSIRAAGG RRGDMVHISY GYGLFTGGLG AHYGAERLGC TVVPMSGGQT EKQVQLIQDF
KPSIIMVTPS YMLNIIEEFQ RQGLDPVASS LKVGIFGAEP WTDAMRAEIQ QRAGIDAVDI
YGLSEVMGPG VASECIESKD GPVIWEDHFY PEIIDPETGE VLPDGEEGEL VFTSLSKEAL
PIIRYRTRDL TRLLPPTSRS MRRIGKITGR SDDMLIIRGV NVFPTQIEEL ICKMPKLAPQ
YQLVISREGH LDKLDVLAEL RPETAAGDVE ALARELQQRI KTNVGVSTTV KLLPPNGIER
TLTGKARRVI DQRPKN
//
