P76084 (PAAI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-coenzyme A thioesterase PaaI
EC=3.1.2.-

Alternative name(s):
Phenylacetic acid degradation protein PaaI

Gene names

Name:	paaI
Synonyms:	ydbV
Ordered Locus Names:	b1396, JW1391

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	140 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3-hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA. Ref.1 Ref.5
Pathway	Aromatic compound metabolism; phenylacetate degradation.
Subunit structure	Homotetramer. Ref.5
Induction	Activated by cAMP receptor protein (CRP), integration host factor (IHF) and by phenylacetyl-coenzyme A (PA-CoA) that prevents PaaX from binding its target sequences. Inhibited by PaaX. Ref.1 Ref.4
Sequence similarities	Belongs to the thioesterase PaaI family.
Biophysicochemical properties	Kinetic parameters: KM=16 µM for 3,4-dihydroxyphenylacetyl-CoA KM=21 µM for 3-hydroxyphenylacetyl-CoA KM=35 µM for 4-hydroxyphenylacetyl-CoA pH dependence: Optimum pH is 7.5-9.
Mass spectrometry	Molecular mass is 14720 Da from positions 2 - 140. Determined by ESI. Ref.5

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phenylacetate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	CoA hydrolase activity Inferred from direct assay Ref.5. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 140

139

Acyl-coenzyme A thioesterase PaaI

PRO_0000156675

Experimental info

Mutagenesis

46

1

N → A: Reduces activity 1000-fold. Ref.5

Mutagenesis

52

1

H → A: Reduces activity 100-fold. Ref.5

Mutagenesis

61

1

D → A: Loss of activity. Ref.5

Secondary structure

1

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140

Helix Strand Turn

Details...

Helix

2 – 22

21

Beta strand

25 – 30

6

Beta strand

33 – 39

7

Helix

42 – 44

3

Beta strand

49 – 51

3

Helix

53 – 69

17

Turn

70 – 72

3

Beta strand

76 – 84

9

Beta strand

93 – 103

11

Beta strand

105 – 115

11

Beta strand

121 – 130

10

Sequences

	Sequence		Length	Mass (Da)
	P76084 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: A91DE9D2C8E8CF42	FASTA	140	14,851
	10 20 30 40 50 60 MSHKAWQNAH AMYENDACAK ALGIDIISMD EGFAVVTMTV TAQMLNGHQS CHGGQLFSLA 70 80 90 100 110 120 DTAFAYACNS QGLAAVASAC TIDFLRPGFA GDTLTATAQV RHQGKQTGVY DIEIVNQQQK 130 140 TVALFRGKSH RIGGTITGEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway." Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M., Garcia J.L., Diaz E. J. Biol. Chem. 273:25974-25986(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PHENYLACETATE CATABOLISM, INDUCTION. Strain: W / ATCC 11105 / DSM 1900.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli." Ferrandez A., Garcia J.L., Diaz E. J. Biol. Chem. 275:12214-12222(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION.
[5]	"Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI." Song F., Zhuang Z., Finci L., Dunaway-Mariano D., Kniewel R., Buglino J.A., Solorzano V., Wu J., Lima C.D. J. Biol. Chem. 281:11028-11038(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-140, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE, FUNCTION, MUTAGENESIS OF ASN-46; HIS-52 AND ASP-61, SUBUNIT.
[6]	"Structure of the E. coli paaI protein from the phyenylacetic acid degradation operon." New York structural genomix research consortium (NYSGXRC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X97452 Genomic DNA. Translation: CAA66098.1.
U00096 Genomic DNA. Translation: AAC74478.1.
AP009048 Genomic DNA. Translation: BAE76427.1.

PIR

G64890.

RefSeq

NP_415914.1. NC_000913.2.
YP_489665.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PSU	X-ray	2.20	A/B	1-140	[»]
2FS2	X-ray	2.00	A/B	2-140	[»]

ProteinModelPortal

P76084.

SMR

P76084. Positions 1-137.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10428N.

IntAct

P76084. 2 interactions.

STRING

511145.b1396.

Protocols and materials databases

DNASU

945265.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74478; AAC74478; b1396.
BAE76427; BAE76427; BAE76427.

GeneID

12932741.
945265.

KEGG

ecj:Y75_p1373.
eco:b1396.

PATRIC

32118078. VBIEscCol129921_1459.

Organism-specific databases

EchoBASE

EB3506.

EcoGene

EG13743. paaI.

Phylogenomic databases

eggNOG

COG2050.

HOGENOM

HOG000066992.

KO

K02614.

OMA

GHGIAHG.

ProtClustDB

CLSK891748.

Enzyme and pathway databases

BioCyc

EcoCyc:G6717-MONOMER.
ECOL316407:JW1391-MONOMER.
MetaCyc:G6717-MONOMER.

UniPathway

UPA00930.

Gene expression databases

Genevestigator

P76084.

Family and domain databases

InterPro

IPR011973. PaaD.
IPR003736. PAAI_dom.
IPR006683. Thioestr_supf.
[Graphical view]

Pfam

PF03061. 4HBT. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02286. PaaD. 1 hit.
TIGR00369. unchar_dom_1. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P76084.

Entry information

Entry name

PAAI_ECOLI

Accession

Primary (citable) accession number: P76084
Secondary accession number(s): Q2MBC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program