PAAK_AROEV
ID PAAK_AROEV Reviewed; 440 AA.
AC Q9L9C1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Phenylacetate-coenzyme A ligase;
DE EC=6.2.1.30;
DE AltName: Full=Phenylacetyl-CoA ligase;
DE Short=PA-CoA ligase;
GN Name=paaK; Synonyms=pacD;
OS Aromatoleum evansii (Azoarcus evansii).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=59406;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, FUNCTION AS A
RP PHENYLACETATE-COENZYME A LIGASE, CATALYTIC ACTIVITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=10629172; DOI=10.1128/jb.182.2.286-294.2000;
RA Mohamed M.E.;
RT "Biochemical and molecular characterization of phenylacetate-coenzyme A
RT ligase, an enzyme catalyzing the first step in aerobic metabolism of
RT phenylacetic acid in Azoarcus evansii.";
RL J. Bacteriol. 182:286-294(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=12172805; DOI=10.1007/s00438-002-0699-9;
RA Rost R., Haas S., Hammer E., Herrmann H., Burchhardt G.;
RT "Molecular analysis of aerobic phenylacetate degradation in Azoarcus
RT evansii.";
RL Mol. Genet. Genomics 267:656-663(2002).
RN [3]
RP FUNCTION AS A PHENYLACETATE-COENZYME A LIGASE AND IN PHENYLACETATE
RP CATABOLISM, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=12189419; DOI=10.1007/s00203-002-0438-y;
RA Mohamed M.E., Ismail W., Heider J., Fuchs G.;
RT "Aerobic metabolism of phenylacetic acids in Azoarcus evansii.";
RL Arch. Microbiol. 178:180-192(2002).
CC -!- FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to
CC phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism.
CC {ECO:0000269|PubMed:10629172, ECO:0000269|PubMed:12189419}.
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:10629172, ECO:0000269|PubMed:12189419};
CC -!- ACTIVITY REGULATION: Inhibition of activity is observed in the presence
CC of a 1 mM of the divalent cations zinc, copper, and nickel.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for PA (aerobically at 37 degrees Celsius)
CC {ECO:0000269|PubMed:10629172, ECO:0000269|PubMed:12189419};
CC KM=45 uM for CoA (aerobically at 37 degrees Celsius)
CC {ECO:0000269|PubMed:10629172, ECO:0000269|PubMed:12189419};
CC KM=60 uM for ATP (aerobically at 37 degrees Celsius)
CC {ECO:0000269|PubMed:10629172, ECO:0000269|PubMed:12189419};
CC pH dependence:
CC Optimum pH is between 8 and 8.5, with a dramatic drop of activity
CC (55%) at pH 9. Less than 10% activity is observed a pH 6, and half
CC the maximal activity is measured at pH 7.
CC {ECO:0000269|PubMed:10629172, ECO:0000269|PubMed:12189419};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. The enzyme is extremely
CC labile, and the activity is totally lost within 48 h at 4 degrees
CC Celsius. {ECO:0000269|PubMed:10629172, ECO:0000269|PubMed:12189419};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10629172}.
CC -!- INDUCTION: Induced by phenylacetate, phenylacetaldehyde, 3-
CC hydroxyphenylacetate, phenylalanine, phenylbutyric acid, DL-
CC phenyllactate, phenylpyruvate, or 4-phenylbutyrate.
CC {ECO:0000269|PubMed:10629172, ECO:0000269|PubMed:12172805}.
CC -!- SIMILARITY: Belongs to the phenylacetyl-CoA ligase family.
CC {ECO:0000305}.
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DR EMBL; AF176259; AAF26285.1; -; Genomic_DNA.
DR EMBL; AJ278756; CAC10605.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9L9C1; -.
DR SMR; Q9L9C1; -.
DR BioCyc; MetaCyc:MON-12132; -.
DR SABIO-RK; Q9L9C1; -.
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; IDA: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 ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding.
FT CHAIN 1..440
FT /note="Phenylacetate-coenzyme A ligase"
FT /id="PRO_0000416773"
SQ SEQUENCE 440 AA; 48735 MW; 28920F3732A34999 CRC64;
MPVKTPSPGD LEPIEKASQD ELRALQLERL KWSVRHAYEN VPHYRKAFDA KGVHPDDLKS
LADLAKFPFT AKGDLRDNYP FGMFAVPREK VARVHASSGT TGKPTVVGYT LKDIDTWATV
VARSIRASGG RAGDMVHIAY GYGLFTGGLG AHYGAEKLGC TVVPMSGGQT EKQIQLIQDF
KPDIIMVTPS YMLTVLDEME RMGIDPHQTS LKVGIFGAEP WTQAMRAAME ARAGIDAVDI
YGLSEVMGPG VANECIEAKD GPVIWEDHFY PEIIDPHTGE VLPDGSEGEL VFTTLTKEAM
PVIRYRTRDL TRLLPPTARS MRRMAKITGR SDDMLIIRGV NLFPTQVEEL ICKNPKLAPQ
YLLEVDKDGH MDTLTVKVEI NPEANVGRHP EQKEALAKEL QHDIKTFIGV SAKVHVCEPF
AIERVTIGKA KRVVDRRPKE
