ID A0A239PVV3_9PROT Unreviewed; 433 AA.
AC A0A239PVV3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN06297382_2149 {ECO:0000313|EMBL:SNT74238.1};
OS Amphiplicatus metriothermophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Amphiplicatus.
OX NCBI_TaxID=1519374 {ECO:0000313|EMBL:SNT74238.1, ECO:0000313|Proteomes:UP000198346};
RN [1] {ECO:0000313|EMBL:SNT74238.1, ECO:0000313|Proteomes:UP000198346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12710 {ECO:0000313|EMBL:SNT74238.1,
RC ECO:0000313|Proteomes:UP000198346};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-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}.
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DR EMBL; FZQA01000004; SNT74238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239PVV3; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000198346; 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:SNT74238.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000198346}.
FT DOMAIN 88..291
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 338..431
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 433 AA; 47557 MW; 2E9EAE882752E195 CRC64;
MPPADYVPLL DDGEKLSEDA LRALQLERLK WSLRHAYENC RPYRAKMEAA GATPDDLKDL
SDLSKFPFTA KDDLRAAYPF GFFAVPMDRI VRLHASSGTT GRPTVVGYTR RDIETWSALM
ARSIRAAGGR PGMKVHVAYG YGLFTGGLGA HYGAEALGCA VIPMSGGQTE KQVRLICDFE
PDVIMVTPSY MLAILDAFRR EGLDPRKSSL RIGIFGAEPW SEAMRGEIET AFDLDAVDIY
GLSEVIGPGV ANECVETKDG LTVWEDHFWP EIVDPETGEP LPEGARGELV LTSLTKEATP
VIRYRTRDLT RLLPGTARVM RRMERITGRT DDMLIVRGVN VFPSQIEEQI LAVPDLAPHY
LLEIARPGRL DELAAIVEAR PGVEGPAREA AARLLAHRVK SLIGVSVAVR IVDPGAIERS
AGKARRVRDL RGA
//
