ID A0A1H9K156_9PSEU Unreviewed; 432 AA.
AC A0A1H9K156;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN04488000_105122 {ECO:0000313|EMBL:SEQ92663.1};
OS Lentzea albida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=65499 {ECO:0000313|EMBL:SEQ92663.1, ECO:0000313|Proteomes:UP000199503};
RN [1] {ECO:0000313|EMBL:SEQ92663.1, ECO:0000313|Proteomes:UP000199503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44437 {ECO:0000313|EMBL:SEQ92663.1,
RC ECO:0000313|Proteomes:UP000199503};
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; FOFV01000005; SEQ92663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9K156; -.
DR STRING; 65499.SAMN04488000_105122; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000199503; 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:SEQ92663.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 94..293
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 339..429
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 432 AA; 47705 MW; FEA1F10F2EA47CF8 CRC64;
MLDLSPQPGD LEPIETASVD ELRALQLERL RWSVRHAYEN VPHYRAAFDT AGVHPDDVKT
LGDLAKLPFT AKADLRDNYP FGMFAVPRQE VVRVHASSGT TGRPTVVGYT RDDLDTWATV
MARSIRAAGG RQGHVLHNAY GYGLFTGGLG AHAGAEKLGC TVVPVSGGMT ERQVQLIRDF
EPDVIMVTPS YMLSIIDEME RQGVDPRSTS LKVGIFGAEP WTNDMRAEME RRLDMHAVDI
YGLSEVIGPG VASECVETKD GLHVWEDHFY PEIIDPVTGE VLPDGEEGEL VFTSLTKQAM
PIIRYRTRDL TRLLPGTARS MRRIEKITGR TDDMIILRGV NLFPTQIEEL ILRVPALSPH
FQCVLSRTGN LDDLTVLVEH REDAVAGDAG AQLRKLVKNS IGVTVAVEVV APGGIERSVG
KMKRIVDRRP PR
//