Reviewed, UniProtKB/Swiss-Prot P23872 (AES_ECOLI)

Names and origin

Protein names

Recommended name:
    Acetyl esterase
    EC=3.1.1.-
Alternative name(s):
    EcE

Gene names

Name:	aes
Synonyms:	ybaC
Ordered Locus Names:	b0476, JW0465

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates malT activity by antagonizing maltotriose binding. Inhibits melA galactosidase activity. Ref.11 Ref.12
Subunit structure	Homodimer. Interacts with malT and melA. Ref.11 Ref.12
Subcellular location	Cytoplasm. HAMAP MF_01958
Miscellaneous	Not essential for cell growth. HAMAP MF_01958
Sequence similarities	Belongs to the 'GDXG' lipolytic enzyme family.
biophysicochemical properties	Kinetic parameters: KM=1.5 mM for p-nitrophenylacetate (at pH 7.1 and 25 degrees Celsius) HAMAP MF_01958 KM=0.7 mM for p-nitrophenylpropionate (at pH 7.1 and 25 degrees Celsius) KM=0.5 mM for p-nitrophenylbutyrate (at pH 7.1 and 25 degrees Celsius) KM=0.26 mM for p-nitrophenylvalerate (at pH 7.1 and 25 degrees Celsius) KM=0.22 mM for p-nitrophenylhexanoate (at pH 7.1 and 25 degrees Celsius) KM=0.16 mM for p-nitrophenyloctanoate (at pH 7.1 and 25 degrees Celsius) Vmax=34.2 µmol/min/mg enzyme toward p-nitrophenylbutyrate (at pH 5.6 and 30 degrees Celsius) Vmax=3.67 µmol/min/mg enzyme toward tributyrylglycerol (at pH 5.6 and 30 degrees Celsius) Vmax=0.22 µmol/min/mg enzyme toward trioleylglycerol (at pH 5.6 and 30 degrees Celsius) pH dependence: Optimum pH is 9.0.
Sequence caution	The sequence L35149 differs from that shown. Reason: Frameshift at position 37.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase Serine esterase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carboxylesterase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 319	319	Acetyl esterase HAMAP MF_01958		PRO_0000071555
Sites
	Active site	165	1	Probable
	Active site	262	1	Probable
	Active site	292	1	Probable
Experimental info
	Mutagenesis	103	1	H → A: Reduces enzymatic efficiency. Ref.10
	Mutagenesis	128	1	E → A: Reduces enzymatic efficiency. Ref.10
	Mutagenesis	163	1	G → A: Diminishes catalytic efficiency. Ref.10
	Mutagenesis	164	1	D → A: Strongly reduces enzymatic activity. Ref.10
	Mutagenesis	165	1	S → A: Abolishes enzymatic activity. Ref.10
	Mutagenesis	167	1	G → A: Diminishes substrate affinity. Ref.10
	Mutagenesis	262	1	D → A: Strongly reduces enzymatic activity. Ref.10
	Mutagenesis	266	1	D → A: Reduces enzymatic efficiency. Ref.10
	Mutagenesis	292	1	H → A: Abolishes enzymatic activity. Ref.10
	Sequence conflict	18	1	K → N Ref.8
	Sequence conflict	275 – 319	45	LAAHQ…FTAQL → VSCASAAL Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P23872-1 [UniParc]. Last modified November 1, 1997. Version 3. Checksum: 4F9E234E23CCE7D0	FASTA	319	36,034
	10 20 30 40 50 60 MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF WNAGAPEMAT 70 80 90 100 110 120 RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG 130 140 150 160 170 180 IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD 190 200 210 220 230 240 KQIDCGKVAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY 250 260 270 280 290 300 CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM 310 MKTADEALRD GAQFFTAQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity." Peist R., Koch A., Bolek P., Sewitz S., Kolbus T., Boos W. J. Bacteriol. 179:7679-7686(1997) [PubMed: 9401025] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12." Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H. J. Mol. Biol. 219:393-398(1991) [PubMed: 2051480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	Miyamoto K. Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Cloning and characterization of the gsk gene encoding guanosine kinase of Escherichia coli." Harlow K.W., Nygaard P., Hove-Jensen B. J. Bacteriol. 177:2236-2240(1995) [PubMed: 7721718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103. Strain: K12.
[8]	Mori H., Iida A., Teshiba S., Fujio T. Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. Strain: K12.
[9]	"An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase." Kanaya S., Koyanagi T., Kanaya E. Biochem. J. 332:75-80(1998) [PubMed: 9576853] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, BIOPHYSICOCHEMICAL PROPERTIES.
[10]	"Identification of catalytically essential residues in Escherichia coli esterase by site-directed mutagenesis." Haruki M., Oohashi Y., Mizuguchi S., Matsuo Y., Morikawa M., Kanaya S. FEBS Lett. 454:262-266(1999) [PubMed: 10431819] [Abstract] Cited for: MUTAGENESIS OF HIS-103; GLU-128; GLY-163; ASP-164; SER-165; GLY-167; ASP-262; ASP-266 AND HIS-292.
[11]	"The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon." Joly N., Danot O., Schlegel A., Boos W., Richet E. J. Biol. Chem. 277:16606-16613(2002) [PubMed: 11867639] [Abstract] Cited for: FUNCTION, INTERACTION WITH MALT.
[12]	"The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism." Mandrich L., Caputo E., Martin B.M., Rossi M., Manco G. J. Biol. Chem. 277:48241-48247(2002) [PubMed: 12374803] [Abstract] Cited for: FUNCTION, DIMERIZATION, INTERACTION WITH MELA.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D90259 Genomic DNA. Translation: BAA14305.2. U82664 Genomic DNA. Translation: AAB40230.1. U00096 Genomic DNA. Translation: AAC73578.1. AP009048 Genomic DNA. Translation: BAE76255.1. D00798 Genomic DNA. No translation available. L35149 Genomic DNA. No translation available.
PIR	C64778.
RefSeq	AP_001125.1. NP_415009.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9062N.
Genome annotation databases
GeneID	947514.
GenomeReviews	Gene locus JW0465 in contig AP009048_GR. Gene locus b0476 in contig U00096_GR.
KEGG	ecj:JW0465. eco:b0476.
Organism-specific databases
EchoBASE	EB1093.
EcoGene	EG11101. aes.
CMR	Search...
Phylogenomic databases
HOGENOM	P23872.
OMA	P23872. ISAGMKT.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11101-MON. MetaCyc:EG11101-MON.
Family and domain databases
HAMAP	MF_01958. [Tree]
InterPro	IPR013094. AB_hydrolase_3. IPR002168. Lipase_GDXG_AS. [Graphical view]
Pfam	PF07859. Abhydrolase_3. 1 hit. [Graphical view]
PROSITE	PS01173. LIPASE_GDXG_HIS. 1 hit. PS01174. LIPASE_GDXG_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AES_ECOLI

Accession

Primary (citable) accession number: P23872
Secondary accession number(s): P77282, Q2MBV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)