PAAK_ECOLI
ID PAAK_ECOLI Reviewed; 437 AA.
AC P76085; O53018; Q2MBC8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Phenylacetate-coenzyme A ligase;
DE EC=6.2.1.30 {ECO:0000269|PubMed:9748275};
DE AltName: Full=Phenylacetyl-CoA ligase;
DE Short=PA-CoA ligase;
GN Name=paaK; OrderedLocusNames=b1398, JW5218;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, AND INDUCTION.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=9748275; DOI=10.1074/jbc.273.40.25974;
RA Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M.,
RA Garcia J.L., Diaz E.;
RT "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a
RT new aerobic hybrid pathway.";
RL J. Biol. Chem. 273:25974-25986(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=10766858; DOI=10.1074/jbc.275.16.12214;
RA Ferrandez A., Garcia J.L., Diaz E.;
RT "Transcriptional regulation of the divergent paa catabolic operons for
RT phenylacetic acid degradation in Escherichia coli.";
RL J. Biol. Chem. 275:12214-12222(2000).
RN [5]
RP FUNCTION AS A PHENYLACETATE-COENZYME A LIGASE.
RX PubMed=20660314; DOI=10.1073/pnas.1005399107;
RA Teufel R., Mascaraque V., Ismail W., Voss M., Perera J., Eisenreich W.,
RA Haehnel W., Fuchs G.;
RT "Bacterial phenylalanine and phenylacetate catabolic pathway revealed.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14390-14395(2010).
CC -!- FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to
CC phenylacetyl-CoA (PA-CoA). {ECO:0000269|PubMed:20660314,
CC ECO:0000269|PubMed:9748275}.
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:9748275};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20957;
CC Evidence={ECO:0000269|PubMed:9748275};
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC {ECO:0000269|PubMed:9748275}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INDUCTION: Activated by cAMP receptor protein (CRP), integration host
CC factor (IHF) and by phenylacetyl-coenzyme A that prevents PaaX from
CC binding its target sequences. Inhibited by PaaX.
CC {ECO:0000269|PubMed:10766858, ECO:0000269|PubMed:9748275}.
CC -!- SIMILARITY: Belongs to the phenylacetyl-CoA ligase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA66100.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X97452; CAA66100.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74480.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76428.1; -; Genomic_DNA.
DR PIR; A64891; A64891.
DR RefSeq; NP_415916.1; NC_000913.3.
DR RefSeq; WP_000632280.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P76085; -.
DR SMR; P76085; -.
DR BioGRID; 4263013; 319.
DR DIP; DIP-10430N; -.
DR STRING; 511145.b1398; -.
DR PaxDb; P76085; -.
DR PRIDE; P76085; -.
DR EnsemblBacteria; AAC74480; AAC74480; b1398.
DR EnsemblBacteria; BAE76428; BAE76428; BAE76428.
DR GeneID; 945963; -.
DR KEGG; ecj:JW5218; -.
DR KEGG; eco:b1398; -.
DR PATRIC; fig|1411691.4.peg.873; -.
DR EchoBASE; EB3508; -.
DR eggNOG; COG1541; Bacteria.
DR HOGENOM; CLU_035301_1_1_6; -.
DR InParanoid; P76085; -.
DR OMA; GVAPHFQ; -.
DR PhylomeDB; P76085; -.
DR BioCyc; EcoCyc:G6719-MON; -.
DR UniPathway; UPA00930; -.
DR PRO; PR:P76085; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IMP:EcoliWiki.
DR GO; GO:0047475; F:phenylacetate-CoA ligase activity; IMP:EcoliWiki.
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 ATP-binding; Direct protein sequencing; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..437
FT /note="Phenylacetate-coenzyme A ligase"
FT /id="PRO_0000058164"
FT VARIANT 127
FT /note="S -> T (in strain: W)"
SQ SEQUENCE 437 AA; 48953 MW; 3D49DB382B80F98A CRC64;
MITNTKLDPI ETASVDELQA LQTQRLKWTL KHAYENVPMY RRKFDAAGVH PDDFRELSDL
RKFPCTTKQD LRDNYPFDTF AVPMEQVVRI HASSGTTGKP TVVGYTQNDI DNWANIVARS
LRAAGGSPKD KIHVAYGYGL FTGGLGAHYG AERLGATVIP MSGGQTEKQA QLIRDFQPDM
IMVTPSYCLN LIEELERQLG GDASGCSLRV GVFGAEPWTQ AMRKEIERRL GITALDIYGL
SEVMGPGVAM ECLETTDGPT IWEDHFYPEI VNPHDGTPLA DGEHGELLFT TLTKEALPVI
RYRTRDLTRL LPGTARTMRR MDRISGRSDD MLIIRGVNVF PSQLEEEIVK FEHLSPHYQL
EVNRRGHLDS LSVKVELKES SLTLTHEQRC QVCHQLRHRI KSMVGISTDV MIVNCGSIPR
SEGKACRVFD LRNIVGA
