Information on EC 3.6.3.18 - oligosaccharide-transporting ATPase:
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The expected taxonomic range for this enzyme is: Agrobacterium tumefaciens

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EC NUMBERCOMMENTARY
3.6.3.18-

RECOMMENDED NAMEGeneOntology No.
oligosaccharide-transporting ATPaseGO:0015422

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + H2O + oligosaccharide/out = ADP + phosphate + oligosaccharide/in
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysis of phosphoric ester----

PATHWAYKEGG LinkMetaCyc Link
alginate degradation-PWY-6986

SYSTEMATIC NAMEIUBMB Comments
ATP phosphohydrolase (disaccharide-importing)ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports lactose, melibiose and raffinose.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
ABC ATPase domain of HlyB transporterEscherichia coli--667495
ABC-type (ATP-binding cassette-type) ATPase----
ATP-binding cassette ATPase domain of the haemolysin B transporterEscherichia coli--667495
HlyB NBDEscherichia coli--667495

CAS REGISTRY NUMBERCOMMENTARY
No entries in this field

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Agrobacterium tumefaciensstrain AR50289128--Manually annotated by BRENDA team
Agrobacterium tumefaciens AR50strain AR50289128--Manually annotated by BRENDA team
Escherichia colistrain DH5alpha667495--Manually annotated by BRENDA team
Escherichia coli DH5alphastrain DH5alpha667495--Manually annotated by BRENDA team
Streptococcus mutans-289127--Manually annotated by BRENDA team
Streptomyces sp.-289129--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
8-azido-ATP + H2O + ?8-azido-ADP + phosphate + ?
show the reaction diagram		Escherichia coli--667495--?
ATP + H2O + ?ADP + phosphate + ?
show the reaction diagram		Escherichia coli--667495--?
ATP + H2O + cellobiose/outADP + phosphate + cellobiose/in
show the reaction diagram		Streptomyces sp.-two separate uptake systems for cellobiose and maltose, the ATP-binding component MsiK assists in cellobiose and maltose transport289129-289129?
ATP + H2O + isomaltotriose/outADP + phosphate + isomaltotriose/in
show the reaction diagram		Streptococcus mutans-the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose289127-289127?
ATP + H2O + lactose/outADP + phosphate + lactose/in
show the reaction diagram		Agrobacterium tumefaciens-lactose transport289128-289128?
ATP + H2O + maltose/outADP + phosphate + maltose/in
show the reaction diagram		Streptomyces sp.-two separate uptake systems for cellobiose and maltose, the ATP-binding component MsiK assists in cellobiose and maltose transport289129-289129?
ATP + H2O + melibiose/outADP + phosphate + melibiose/in
show the reaction diagram		Streptococcus mutans-the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose289127-289127?
ATP + H2O + raffinose/outADP + phosphate + raffinose/in
show the reaction diagram		Streptococcus mutans-the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose289127-289127?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + H2O + isomaltotriose/outADP + phosphate + isomaltotriose/in
show the reaction diagram		Streptococcus mutans-the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose289127-289127
ATP + H2O + lactose/outADP + phosphate + lactose/in
show the reaction diagram		Agrobacterium tumefaciens-lactose transport289128-289128
ATP + H2O + melibiose/outADP + phosphate + melibiose/in
show the reaction diagram		Streptococcus mutans-the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose289127-289127
ATP + H2O + raffinose/outADP + phosphate + raffinose/in
show the reaction diagram		Streptococcus mutans-the enzyme system is responsible for the uptake of melibiose, raffinose and isomaltotriose289127-289127

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Mg2+Escherichia coli-100% activity at pH 8.0 and with 10 mM KCl667495
Mn2+Escherichia coli-125% activity at pH 8.0 and with 10 mM KCl667495

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Ca2+Escherichia coli-3% activity at pH 8.0 and 10 mM KCl667495 2D-image
OrthovanadateEscherichia coli-0.005-0.05 mM, pH 8.0, IC50: 0.016 mM667495 2D-image
Zn2+Escherichia coli-1% activity at pH 8.0 and 10 mM KCl667495 2D-image
Co2+Escherichia coli-47% activity at pH 8.0 and 10 mM KCl667495 2D-image
additional informationEscherichia coli-the activity is reversibly inhibited by high salt concentrations in the physiologically range accompanied by proportional decreased binding of 8-azido-ATP (3-5% residual activity at 200-300 mM salt)667495-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.65-ATPEscherichia coli-KM-value with 50% of the enzyme being substrate-saturated, in the presence of 10 mM NaCl667495 2D-image
1.09-ATPEscherichia coli-KM-value with 50% of the enzyme being substrate-saturated, in the presence of 50 mM NaCl667495 2D-image
1.5-ATPEscherichia coli-KM-value with 50% of the enzyme being substrate-saturated, in the presence of 100 mM NaCl667495 2D-image
2.33-ATPEscherichia coli-KM-value with 50% of the enzyme being substrate-saturated, in the presence of 200 mM NaCl667495 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.11-ATPEscherichia coli-KM-value with 50% of the enzyme being substrate-saturated, in the presence of 200 mM NaCl667495 2D-image
0.2-ATPEscherichia coli-KM-value with 50% of the enzyme being substrate-saturated, in the presence of 100 mM NaCl667495 2D-image
0.31-ATPEscherichia coli-KM-value with 50% of the enzyme being substrate-saturated, in the presence of 50 mM NaCl667495 2D-image
0.33-ATPEscherichia coli-KM-value with 50% of the enzyme being substrate-saturated, in the presence of 10 mM NaCl667495 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.016-OrthovanadateEscherichia coli-0.005-0.05 mM, pH 8.0, IC50: 0.016 mM667495 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
8-Escherichia coli-in the presence of 3 mM MgCl2 and 10 mM KCl667495

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
78.5Escherichia coli--667495

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
periplasmStreptococcus mutans, Streptococcus mutans 6715, Streptococcus mutans AHT, Streptococcus mutans BHT, Streptococcus mutans E49, Streptococcus mutans HS6, Streptococcus mutans JC2, Streptococcus mutans K1-R, Streptococcus mutans OMZ 176---289127Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
27500-Escherichia coli-HlyB NBD in the presence of 100 mM KCl and ATP, ultracentrifugation667495
27700-Escherichia coli-HlyB NBD in the presence of 10 mM KCl and in the absence of ATP, ultracentrifugation667495
28000-Escherichia coli-His-tagged HlyB ABC domain, gel filtration667495
30800-Escherichia coli-HlyB NBD in the presence of 10 mM KCl and ATP, ultracentrifugation667495
35700-Escherichia coli-HlyB NBD in the absence of KCl and ATP, ultracentrifugation667495

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerEscherichia coli-2 * 28000, gel filtration, small amounts of dimers (apparently when stabilized by 8-azido-ATP) are detected even in the presence of salt667495
monomerEscherichia coli-1 * 28000, gel filtration and ultracentrifugation, over a wide range of protein or NaCl or KCl concentrations the enzyme is only detected as monomer667495
additional informationStreptococcus mutans-the proteins specified by the msm operon includes: 1. alpha-galactosidase, aga, MW 32050 Da determined by calculation from nucleotide sequence, 2. a periplasmic-like sugar-binding protein, msmE, MW 31900 Da determined by calculation from nucleotide sequence, 3.+ 4. two membrane proteins, msmF and msmG, MW for both is 28500 DA as determined by SDS-PAGE, MW 31615 Da for msmG determined by calculation from nucleotide sequence, 5. sucrose phosphorylase, gtfA, 6. an ATP-binding protein, msmK, MW 41960 Da determined by calculation from nucleotide sequence, MW 35000 Da determined by SDS-PAGE and 7. a dextran glucosidase, dexB, MW 48000 Da determined by SDS-PAGE. The operon is controlled by the regulatory gene msmR, MW 26000 Da, determined by SDS-PAGE289127
additional informationAgrobacterium tumefaciens-lac operon encodes a binding-protein-dependent lactose transport system and beta-galactosidase: 1. lactose binding protein, lacE, MW 42992 calculated from amino acid sequence, 2. integral membrane protein LacF, 3. integral membrane protein lacG, 4. an ATP-binding protein, lacK, MW 39299 calculated from nucleotide sequence, 5. beta galactosidase, lacZ289128
additional informationStreptomyces sp.-two separate uptake systems for cellobiose and maltose, the ATP-binding component MsiK assists in cellobiose and maltose transport289129

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
proteolytic modificationAgrobacterium tumefaciens, Agrobacterium tumefaciens 30147, Agrobacterium tumefaciens 30150, Agrobacterium tumefaciens 47C, Agrobacterium tumefaciens AD1, Agrobacterium tumefaciens AKU, Agrobacterium tumefaciens AKU 0300, Agrobacterium tumefaciens AR50, Agrobacterium tumefaciens ATCC 15955, Agrobacterium tumefaciens B-261, Agrobacterium tumefaciens B3/73, Agrobacterium tumefaciens B6-6, Agrobacterium tumefaciens BQL9, Agrobacterium tumefaciens CCRC 14924, Agrobacterium tumefaciens CIP 67.1, Agrobacterium tumefaciens D3, Agrobacterium tumefaciens DUL-DH101, Agrobacterium tumefaciens GV4R10c21, Agrobacterium tumefaciens IAM 1525, Agrobacterium tumefaciens IAM 1526, Agrobacterium tumefaciens IAM B-261, Agrobacterium tumefaciens IAM13299, Agrobacterium tumefaciens ICR, Agrobacterium tumefaciens J14a, Agrobacterium tumefaciens K-28, Agrobacterium tumefaciens K84, Agrobacterium tumefaciens KCCM 10413, Agrobacterium tumefaciens M-1, Agrobacterium tumefaciens NRRL, Agrobacterium tumefaciens NRRL B11291, Agrobacterium tumefaciens NTRRL B11291, Agrobacterium tumefaciens R10, Agrobacterium tumefaciens RS5, Agrobacterium tumefaciens S2, Agrobacterium tumefaciens S33, Agrobacterium tumefaciens ST96-4, Agrobacterium tumefaciens YH-2-LacE is synthesized as a precursor protein of 422 amino acids, the mature protein is formed by cleavage of the 28 amino acid-N-terminal region289128
proteolytic modificationStreptococcus mutans, Streptococcus mutans 6715, Streptococcus mutans AHT, Streptococcus mutans BHT, Streptococcus mutans E49, Streptococcus mutans HS6, Streptococcus mutans JC2, Streptococcus mutans K1-R, Streptococcus mutans OMZ 176-the msmE gene encodes a proteins of 420 amino acids, the first 22 specifying a signal peptide289127

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
7-Escherichia coli-75% activity in the presence of 3 mM MgCl2 and 10 mM KCl667495
7.5-Escherichia coli-90% activity in the presence of 3 mM MgCl2 and 10 mM KCl667495
8-Escherichia coli-100% activity in the presence of 3 mM MgCl2 and 10 mM KCl667495
8.5-Escherichia coli-85% activity in the presence of 3 mM MgCl2 and 10 mM KCl667495

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-80°C, 50 mM phosphate buffer pH 8, 50 mM KCl and 10% glycerol, 15 mg/ml HlyB ABC domain, indefinite storage duration, no loss of activityEscherichia coli-667495
-80°C, phosphate or Tris buffer pH 8, in the absence of ATP, up to 25 mg/ml His-tagged HlyB ABC domain, indefinite storage duration, no loss of activityEscherichia coli-667495
25°C, 50 mM phosphate buffer pH 8, 50 mM KCl and 10% glycerol, 15 mg/ml HlyB ABC domain, 24h, 20% loss of activityEscherichia coli-667495
4°C, 50 mM phosphate buffer pH 8, 50 mM KCl and 10% glycerol, 15 mg/ml HlyB ABC domain, 2 days, no loss of activityEscherichia coli-667495
4°C, phosphate or Tris buffer pH 8, in the absence of ATP, up to 25 mg/ml His-tagged HlyB ABC domain, at least 2 days, no loss of activityEscherichia coli-667495

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
HlyB ABC domain, Ni2+-chelating Sepharose 16/20 fast flow column chromatography, His-tagged HlyB ABC domain, immobilized metal-affinity chromatographyEscherichia coli-667495

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coliAgrobacterium tumefaciens-289128

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
289127Russell, R.R.B.; Aduse-Opoku, J.; Sutcliffe, I.C.; Tao, L.; Ferretti, J.J.A binding protein-dependent transport system in Streptococcus mutans responsible for multiple sugar metabolismJ. Biol. Chem.2674631-46371992Streptococcus mutans PubMed
289128Williams, S.G.; Greenwood, J.A.; Jones, C.W.Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and beta-galactosidase in Agrobacterium radiobacterMol. Microbiol.61755-17681992Agrobacterium tumefaciens, Agrobacterium tumefaciens AR50 PubMed
289129Schloesser, A.; Kampers, T.; Schrempf, H.The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transportJ. Bacteriol.1792092-20951997Streptomyces sp. PubMed
667495Benabdelhak, H.; Schmitt, L.; Horn, C.; Jumel, K.; Blight, M.A.; Holland, I.B.Positive co-operative activity and dimerization of the isolated ABC ATPase domain of HlyB from Escherichia coliBiochem. J.386489-4952005Escherichia coli, Escherichia coli DH5alpha PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 3.6.3.18)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)