ID A0A1I5QX02_9PSEU Unreviewed; 445 AA.
AC A0A1I5QX02;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN05421810_102794 {ECO:0000313|EMBL:SFP50834.1};
OS Amycolatopsis arida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=587909 {ECO:0000313|EMBL:SFP50834.1, ECO:0000313|Proteomes:UP000198727};
RN [1] {ECO:0000313|Proteomes:UP000198727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5579 {ECO:0000313|Proteomes:UP000198727};
RA Varghese N., Submissions S.;
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; FOWW01000002; SFP50834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5QX02; -.
DR STRING; 587909.SAMN05421810_102794; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000198727; 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:SFP50834.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000198727}.
FT DOMAIN 106..301
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 349..442
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 445 AA; 49368 MW; AFAD840CA98BD041 CRC64;
MTTTPDDVAS APAGVDTVEL DAGERLGGDE LRALHLKRLQ WTLRHAYRNV PHYRRKFDEA
GVHPDDCRSL ADLAKFPFTT KEDLRQTYPF GMFAVSRERV RRIHASSGTT GKPTVVGYTE
RDLANWAEVM ARSIRAAGGR PGQMVHVAYG YGLFTGGLGA HYGAERLGCT VVPASGGMTA
RQVRLITDFR PEVVMVTPSY MLTLLDEFER QGIDPRRTSL RVGIFGAEPW TEAMRAEIEE
RGGIDAVDIY GLSEVMGPGV AQECVETKDG LHIWEDHFYP EVIDPIEGTV LADGESGELV
FTSLTKEALP IIRYRTRDLT RLLPGTARPA HRRMAKVTGR SDDMIILRGV NLFPTQIEEM
VLGTTGLSPH FQLVLTTRER LDHLTVRVEA RADTPAERRP AAAAELADRV KDGVGVSVDV
EVTDPETLER SVGKLRRIVD QRENR
//
