ID A0A1C3MZT7_9ACTN Unreviewed; 435 AA.
AC A0A1C3MZT7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=GA0070620_1322 {ECO:0000313|EMBL:SBV25840.1};
OS Micromonospora krabiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=307121 {ECO:0000313|EMBL:SBV25840.1, ECO:0000313|Proteomes:UP000199393};
RN [1] {ECO:0000313|Proteomes:UP000199393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45344 {ECO:0000313|Proteomes:UP000199393};
RA Varghese N.;
RL Submitted (JUN-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; LT598496; SBV25840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3MZT7; -.
DR STRING; 307121.GA0070620_1322; -.
DR PATRIC; fig|307121.4.peg.1356; -.
DR OrthoDB; 580775at2; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000199393; Chromosome i.
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:SBV25840.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444};
KW Reference proteome {ECO:0000313|Proteomes:UP000199393}.
FT DOMAIN 86..292
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 339..432
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 435 AA; 48873 MW; 0C9A5EA5F9C95262 CRC64;
MRDRTPRPED LEPIERASVD ELRSVQRERL RWSLRHAYDN VPHYRRAFDA AQVHPDDLRD
LDDLARFPFT GKAELRENYP FGMFAVPREQ VARLHASSGT TGRPTVVGYT RADLTTWARL
MARSIRASGG RPGDRVHVAY GYGLFTGGLG AHYGAEEMGC TVIPVSGGMT ERQVMLIRDF
EPEVIMVTPS YLLAIVDEME RQGVDPRTTS LEVGIFGAEP WTEDMRREME QRLDMHAVDI
YGLSEVMGPG VANECVETKD GLHLWEDHFY PEIIDPVTGA VLPDGERGEL VLTSLTKEAM
PVVRYRTRDL TRLLPGTARP MRRIEKITGR TDDMMIVRGV NVFPTQIEEL ILRTPELSPH
FQCVLDRQGR MDTLTVRVER RVGVAVDAAQ RAGAALVELV KNTVGVSVAV DVIAPDGVER
SMGKMRRIVD QRRAG
//
