ID A0A1H0LT02_9ACTN Unreviewed; 446 AA.
AC A0A1H0LT02;
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=SAMN05428965_0038 {ECO:0000313|EMBL:SDO71225.1};
OS Geodermatophilus sp. DSM 45219.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1881103 {ECO:0000313|EMBL:SDO71225.1, ECO:0000313|Proteomes:UP000198730};
RN [1] {ECO:0000313|EMBL:SDO71225.1, ECO:0000313|Proteomes:UP000198730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45219 {ECO:0000313|EMBL:SDO71225.1,
RC ECO:0000313|Proteomes:UP000198730};
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; FNIQ01000010; SDO71225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0LT02; -.
DR STRING; 1881103.SAMN05428965_0038; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000198730; 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:SDO71225.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 107..303
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 350..443
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 446 AA; 49690 MW; 67FB6AEF76B1151B CRC64;
MTAVTSETPR RLGARPDEAI LDPAERMSVD ELRALQLERL QWTLRHAYEN VPHYRQALDA
AGVHPDDCRE LSDLARFPTT SKADLRDNYP FGMFAVPQEQ VRRVHASSGT TGRPTVVGYT
ERDIDTWATV MARSIRAAGG RAGDKLHNAY GYGLFTGGLG AHYGAEKLGC TVIPVSGGMT
PRQVQLITDF APRVVMVTPS YMLTVIDEFE KQGIDPRSSS LEIGIFGAEP WTEQMRREME
DRLDIEAVDI YGLSEVMGPG VAQECVETKD GLHVWEDHFY PEVIDPLTGE VLPEGEQGEL
VFTSLTKEAM PVIRYRTRDL TRLLPGTARP GMRRMEKITG RTDDMIILRG VNLFPTQIEE
IVLRTPGLSP HFALELTTRG RMDHLTCRVE ARPDCPAERR PVAAAEVAKA VKDTVGTSIE
VLVVDPETLA RSVGKLKRLY DHRDRA
//
