PAAI_ECOLI
ID PAAI_ECOLI Reviewed; 140 AA.
AC P76084; Q2MBC9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Acyl-coenzyme A thioesterase PaaI;
DE EC=3.1.2.-;
DE AltName: Full=Phenylacetic acid degradation protein PaaI;
GN Name=paaI; Synonyms=ydbV; OrderedLocusNames=b1396, JW1391;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHENYLACETATE CATABOLISM,
RP 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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-140, MASS SPECTROMETRY, CLEAVAGE
RP OF INITIATOR METHIONINE, FUNCTION, MUTAGENESIS OF ASN-46; HIS-52 AND
RP ASP-61, AND SUBUNIT.
RX PubMed=16464851; DOI=10.1074/jbc.m513896200;
RA Song F., Zhuang Z., Finci L., Dunaway-Mariano D., Kniewel R., Buglino J.A.,
RA Solorzano V., Wu J., Lima C.D.;
RT "Structure, function, and mechanism of the phenylacetate pathway hot dog-
RT fold thioesterase PaaI.";
RL J. Biol. Chem. 281:11028-11038(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Structure of the E. coli paaI protein from the phyenylacetic acid
RT degradation operon.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Thioesterase with a preference for ring-hydroxylated
CC phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3-
CC hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards
CC 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA.
CC {ECO:0000269|PubMed:16464851, ECO:0000269|PubMed:9748275}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for 3,4-dihydroxyphenylacetyl-CoA;
CC KM=21 uM for 3-hydroxyphenylacetyl-CoA;
CC KM=35 uM for 4-hydroxyphenylacetyl-CoA;
CC pH dependence:
CC Optimum pH is 7.5-9.;
CC -!- PATHWAY: Aromatic compound metabolism; phenylacetate degradation.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16464851}.
CC -!- INDUCTION: Activated by cAMP receptor protein (CRP), integration host
CC factor (IHF) and by phenylacetyl-coenzyme A (PA-CoA) that prevents PaaX
CC from binding its target sequences. Inhibited by PaaX.
CC {ECO:0000269|PubMed:10766858, ECO:0000269|PubMed:9748275}.
CC -!- MASS SPECTROMETRY: Mass=14720; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16464851};
CC -!- SIMILARITY: Belongs to the thioesterase PaaI family. {ECO:0000305}.
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DR EMBL; X97452; CAA66098.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74478.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76427.1; -; Genomic_DNA.
DR PIR; G64890; G64890.
DR RefSeq; NP_415914.1; NC_000913.3.
DR RefSeq; WP_000018413.1; NZ_STEB01000005.1.
DR PDB; 1PSU; X-ray; 2.20 A; A/B=1-140.
DR PDB; 2FS2; X-ray; 2.00 A; A/B=2-140.
DR PDBsum; 1PSU; -.
DR PDBsum; 2FS2; -.
DR AlphaFoldDB; P76084; -.
DR SMR; P76084; -.
DR BioGRID; 4261735; 619.
DR DIP; DIP-10428N; -.
DR IntAct; P76084; 2.
DR STRING; 511145.b1396; -.
DR PaxDb; P76084; -.
DR PRIDE; P76084; -.
DR DNASU; 945265; -.
DR EnsemblBacteria; AAC74478; AAC74478; b1396.
DR EnsemblBacteria; BAE76427; BAE76427; BAE76427.
DR GeneID; 66674747; -.
DR GeneID; 945265; -.
DR KEGG; ecj:JW1391; -.
DR KEGG; eco:b1396; -.
DR PATRIC; fig|1411691.4.peg.875; -.
DR EchoBASE; EB3506; -.
DR eggNOG; COG2050; Bacteria.
DR HOGENOM; CLU_089876_11_0_6; -.
DR InParanoid; P76084; -.
DR OMA; FACNSHN; -.
DR PhylomeDB; P76084; -.
DR BioCyc; EcoCyc:G6717-MON; -.
DR BioCyc; MetaCyc:G6717-MON; -.
DR BRENDA; 3.1.2.B5; 2026.
DR UniPathway; UPA00930; -.
DR EvolutionaryTrace; P76084; -.
DR PRO; PR:P76084; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016289; F:CoA hydrolase activity; IDA:EcoCyc.
DR GO; GO:0010124; P:phenylacetate catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR011973; PaaD.
DR InterPro; IPR003736; PAAI_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR02286; PaaD; 1.
DR TIGRFAMs; TIGR00369; unchar_dom_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16464851"
FT CHAIN 2..140
FT /note="Acyl-coenzyme A thioesterase PaaI"
FT /id="PRO_0000156675"
FT MUTAGEN 46
FT /note="N->A: Reduces activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:16464851"
FT MUTAGEN 52
FT /note="H->A: Reduces activity 100-fold."
FT /evidence="ECO:0000269|PubMed:16464851"
FT MUTAGEN 61
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16464851"
FT HELIX 2..22
FT /evidence="ECO:0007829|PDB:2FS2"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2FS2"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2FS2"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2FS2"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2FS2"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:2FS2"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2FS2"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:2FS2"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:2FS2"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:2FS2"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:2FS2"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1PSU"
SQ SEQUENCE 140 AA; 14851 MW; A91DE9D2C8E8CF42 CRC64;
MSHKAWQNAH AMYENDACAK ALGIDIISMD EGFAVVTMTV TAQMLNGHQS CHGGQLFSLA
DTAFAYACNS QGLAAVASAC TIDFLRPGFA GDTLTATAQV RHQGKQTGVY DIEIVNQQQK
TVALFRGKSH RIGGTITGEA
