ID A2VT83_9BURK Unreviewed; 432 AA.
AC A2VT83;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=BCPG_01183 {ECO:0000313|EMBL:EAY62929.1};
OS Burkholderia cenocepacia PC184.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350702 {ECO:0000313|EMBL:EAY62929.1, ECO:0000313|Proteomes:UP000053735};
RN [1] {ECO:0000313|EMBL:EAY62929.1, ECO:0000313|Proteomes:UP000053735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC184 {ECO:0000313|EMBL:EAY62929.1,
RC ECO:0000313|Proteomes:UP000053735};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., Crawford M.,
RA Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., White J.,
RA Larson L., Alvarado L., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA LiPuma J., Lory S.;
RT "The Genome Sequence of Burkholderia cenocepacia (strain PC184).";
RL Submitted (DEC-2005) 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; CH482377; EAY62929.1; -; Genomic_DNA.
DR AlphaFoldDB; A2VT83; -.
DR HOGENOM; CLU_035301_1_1_4; -.
DR UniPathway; UPA00930; -.
DR Proteomes; UP000053735; 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};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR006444}.
FT DOMAIN 82..289
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 335..430
FT /note="AMP-dependent ligase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14535"
SQ SEQUENCE 432 AA; 47642 MW; F00351580C86D9D5 CRC64;
MTTPLPLEPI ETASRDELTA LQLERLKWSL RHAYDHSPVY RRKFDEAGVH PDDVTTLADL
SRFPFTTKGD LRDSYPFGMF AVPQDQISRI HASSGTTGKP TVVGYTAADI DTWANLVARS
IRAAGARRGD KVHVSYGYGL FTGGLGAHYG AERAGLTVIP FGGGQTEKQV QLIQDFRPDI
IMVTPSYMLS IADEIERQGL DPVQSSLRIG IFGAEPWTND MRVAIEQRMG IDAVDIYGLS
EVMGPGVASE CVETKDGPTI WEDHFYPEII DPETGEVLPD GELGELVFTS LTKEALPIIR
YRTRDLTRLL PGTARTMRRM EKITGRSDDM MIVRGVNVFP TQIEEQLLKQ RALAPHYQIV
LTKEGPLDVL TLNVEPCPET APDTAAIQAA KQALAYDIKS LIGVTAVINV LPVNGIERSV
GKARRVIDKR KS
//
