PAAK_PSEPU
ID PAAK_PSEPU Reviewed; 439 AA.
AC O33469;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Phenylacetate-coenzyme A ligase;
DE EC=6.2.1.30 {ECO:0000269|PubMed:2324116};
DE AltName: Full=Phenylacetyl-CoA ligase {ECO:0000303|PubMed:2324116};
DE Short=PA-CoA ligase {ECO:0000303|PubMed:2324116};
GN Name=paaK;
GN Synonyms=paaF {ECO:0000312|EMBL:AAC24333.2},
GN pcl {ECO:0000303|PubMed:8969218}, phaE {ECO:0000303|PubMed:9600981};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHENYLACETATE CATABOLISM,
RP AND PATHWAY.
RC STRAIN=U;
RX PubMed=8969218; DOI=10.1074/jbc.271.52.33531;
RA Minambres B., Martinez-Blanco H., Olivera E.R., Garcia B., Diez B.,
RA Barredo J.L., Moreno M.A., Schleissner C., Salto F., Luengo J.M.;
RT "Molecular cloning and expression in different microbes of the DNA encoding
RT Pseudomonas putida U phenylacetyl-CoA ligase. Use of this gene to improve
RT the rate of benzylpenicillin biosynthesis in Penicillium chrysogenum.";
RL J. Biol. Chem. 271:33531-33538(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHENYLACETATE CATABOLISM,
RP PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=U;
RX PubMed=9600981; DOI=10.1073/pnas.95.11.6419;
RA Olivera E.R., Minambres B., Garcia B., Muniz C., Moreno M.A., Ferrandez A.,
RA Diaz E., Garcia J.L., Luengo J.M.;
RT "Molecular characterization of the phenylacetic acid catabolic pathway in
RT Pseudomonas putida U: the phenylacetyl-CoA catabolon.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6419-6424(1998).
RN [3]
RP FUNCTION AS A PHENYLACETYL-COA LIGASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP AND INDUCTION.
RC STRAIN=U;
RX PubMed=2324116; DOI=10.1016/s0021-9258(19)39262-2;
RA Martinez-Blanco H., Reglero A., Rodriguez-Aparicio L.B., Luengo J.M.;
RT "Purification and biochemical characterization of phenylacetyl-CoA ligase
RT from Pseudomonas putida. A specific enzyme for the catabolism of
RT phenylacetic acid.";
RL J. Biol. Chem. 265:7084-7090(1990).
CC -!- FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to
CC phenylacetyl-CoA (PA-CoA) (PubMed:2324116). Involved in the
CC phenylalanine metabolism (PubMed:2324116, PubMed:8969218,
CC PubMed:9600981). Can also use CTP and UTP as substrate
CC (PubMed:2324116). {ECO:0000269|PubMed:2324116,
CC ECO:0000269|PubMed:8969218, ECO:0000269|PubMed:9600981}.
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:0000269|PubMed:2324116};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20957;
CC Evidence={ECO:0000269|PubMed:2324116};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cations (zinc, copper,
CC mercury) and by the sulfhydryl reagents 5,5-dithiobis(2-nitrobenzoic
CC acid), N-ethylmaleimide and p-chloromercuribenzoate.
CC {ECO:0000269|PubMed:2324116}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.7 mM for ATP (at 30 degrees Celsius and pH 8.2)
CC {ECO:0000269|PubMed:2324116};
CC KM=1 mM for CoA (at 30 degrees Celsius and pH 8.2)
CC {ECO:0000269|PubMed:2324116};
CC KM=16.5 mM for PA (at 30 degrees Celsius and pH 8.2)
CC {ECO:0000269|PubMed:2324116};
CC pH dependence:
CC Optimum pH is 8.2. {ECO:0000269|PubMed:2324116};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. The enzyme is heat stable.
CC {ECO:0000269|PubMed:2324116};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC {ECO:0000305|PubMed:8969218, ECO:0000305|PubMed:9600981}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9L9C1}.
CC -!- INDUCTION: Induced by phenylacetate. {ECO:0000269|PubMed:2324116,
CC ECO:0000269|PubMed:9600981}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not activate PA to PA-CoA but can
CC completely catabolize all molecules that synthesize PA-CoA through
CC other routes. {ECO:0000269|PubMed:9600981}.
CC -!- SIMILARITY: Belongs to the phenylacetyl-CoA ligase family.
CC {ECO:0000305}.
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DR EMBL; AF029714; AAC24333.2; -; Genomic_DNA.
DR RefSeq; WP_059394932.1; NZ_QLLF01000010.1.
DR AlphaFoldDB; O33469; -.
DR SMR; O33469; -.
DR KEGG; ag:AAC24333; -.
DR UniPathway; UPA00930; -.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0047475; F:phenylacetate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0010124; P:phenylacetate catabolic process; IMP:UniProtKB.
DR CDD; cd05913; PaaK; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR028154; AMP-dep_Lig_C.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR011880; PA_CoA_ligase.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF14535; AMP-binding_C_2; 1.
DR PIRSF; PIRSF006444; PaaK; 1.
DR TIGRFAMs; TIGR02155; PA_CoA_ligase; 1.
PE 1: Evidence at protein level;
KW Ligase; Nucleotide-binding.
FT CHAIN 1..439
FT /note="Phenylacetate-coenzyme A ligase"
FT /id="PRO_0000416775"
SQ SEQUENCE 439 AA; 49392 MW; 9DE2606A12932B73 CRC64;
MNMYHDADRA LLDPMETASV DALRQHQLER LRWSLKHAYD NVPLYRQRFA ECGAHPDDLT
CLEDLAKFPF TGKNDLRDNY PYGMFAVPQE EVVRLHASSG TTGKPTVVGY TQNDINTWAN
VVARSIRAAG GRKGDKVHVS YGYGLFTGGL GAHYGAERLG CTVIPMSGGQ TEKQVQLIRD
FQPDIIMVTP SYMLNLADEI ERQGIDPHDL KLRLGIFGAE PWTDELRRSI EQRLGINALD
IYGLSEIMGP GVAMECIETK DGPTIWEDHF YPEIIDPVTG EVLPDGQLGE LVFTSLSKEA
LPMVRYRTRD LTRLLPGTAR PMRRIGKITG RSDDMLIIRG VNVFPTQIEE QVLKIKQLSE
MYEIHLYRNG NLDSVEVHVE LRAECQHLDE GQRKLVIGEL SKQIKTYIGI STQVHLQACG
TLKRSEGKAC HVYDKRLAS
