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Information on EC 7.5.2.3 - ABC-type beta-glucan transporter
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7.5.2.3 ABC-type beta-glucan transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. An enzyme found in Gram-negative bacteria that exports beta-glucans.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
so-bp, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-glucan-transporting ATPase
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EC 3.6.3.42
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formerly
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + beta-glucan[side 1] = ADP + phosphate + beta-glucan[side 2]
ABC-type (ATP-binding cassette) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An enzyme found in Gram-negative bacteria that exports beta-glucan
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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transmembrane export
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, beta-glucan-exporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. An enzyme found in Gram-negative bacteria that exports beta-glucans.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + beta-glucan[side 1]
ADP + phosphate + beta-glucan[side 2]
chain length specificity of Lin1841, key factor determining the specificity for chain length of ligands is the polar interactions toward unit C. SO-BP binds to Sopns with energetically favorable conformations
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ATP + H2O + sophoropentasaccharide[side 1]
ADP + phosphate + sophoropentasaccharide[side 2]
substrate Sop5
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?
ATP + H2O + sophorotetrasaccharide[side 1]
ADP + phosphate + sophorotetrasaccharide[side 2]
substrate Sop4
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?
ATP + H2O + sophorotrisaccharide[side 1]
ADP + phosphate + sophorotrisaccharide[side 2]
substrate Sop3
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ATP + H2O + succinoglycan/in
ADP + phosphate + succinoglycan/out
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ATP + H2O + beta-1,2-glucan/in
ADP + phosphate + beta-1,2-glucan/out
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ATP + H2O + beta-1,2-glucan/in
ADP + phosphate + beta-1,2-glucan/out
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ATP + H2O + beta-glucan/in
ADP + phosphate + beta-glucan/out
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ATP + H2O + beta-glucan/in
ADP + phosphate + beta-glucan/out
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additional information
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Sopn-binding protein (SO-BP) specifically binds to shorter oligosaccharides (Sopns) with a degree of polymerization of 3 or more, with Kd values in the micromolar range. The enzyme also binds to larger linear beta-1,2-glucans (average DP 25)
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additional information
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Sopn-binding protein (SO-BP) specifically binds to shorter oligosaccharides (Sopns) with a degree of polymerization of 3 or more, with Kd values in the micromolar range. The enzyme also binds to larger linear beta-1,2-glucans (average DP 25)
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + succinoglycan/in
ADP + phosphate + succinoglycan/out
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ATP + H2O + beta-1,2-glucan/in
ADP + phosphate + beta-1,2-glucan/out
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ATP + H2O + beta-1,2-glucan/in
ADP + phosphate + beta-1,2-glucan/out
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ATP + H2O + beta-glucan/in
ADP + phosphate + beta-glucan/out
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ATP + H2O + beta-glucan/in
ADP + phosphate + beta-glucan/out
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
sophorooligosaccharide binding kinetics and thermodynamics of wild-type Lin1841 and mutants, overview
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additional information
additional information
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sophorooligosaccharide binding kinetics and thermodynamics of wild-type Lin1841 and mutants, overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the ABC uptake system associated with SO-BP is conserved in a number of bacterial species in firmicutes, actinobacteria, and proteobacteria. Consensus phylogenetic tree of SO-BP homologues, the phylogenetic tree is constructed using the neighbor-joining method, overview
physiological function
ATP-binding cassette (ABC)2-type transporters are widely distributed in living organisms, forming one of the largest protein superfamilies. ABC transporters utilize the free energy obtained from ATP hydrolysis to import or export a wide variety of molecules across cellular membranes. They share a common architecture consisting of two transmembrane domains (TMDs) and intracellular nucleotide-binding domains (NBDs). In bacterial ABC importers, an additional domain, a solute (or substrate)-binding protein (SBP), serves as an initial receptor that specifically binds to ligands with high affinity, delivers them to TMDs, and stimulates the ATPase activity. Genes Lin1841 and Lin1842-1843 from the Gram-positive bacterium Listeria innocua encode an SBP and TMDs, respectively. The transporter is responsible for uptake of beta-1,2-Glucan and its shorter oligosaccharides (sophorooligosaccharides, Sopns). beta-1,2-Glucans are bacterial carbohydrates that exist in cyclic or linear forms and play an important role in infections and symbioses involving Gram-negative bacteria. Sopns are captured and imported into the bacterial cell by Sopn-binding protein (SO-BP, Lin1841) associated with the ATP-binding cassette (ABC) transporter. A key factor determining the specificity for chain length of ligands is the polar interactions toward unit C
additional information
additional information
the complex structures with substrates Sop3-5s bound can be overlaid well, molecular dynamics and three-dimensional structure modeling, architecture of the ligand-binding site, overview. Hydrogen bonds play a pivotal role in stabilizing the SO-BP-Sopn complexes. Thr95, Thr96, Glu147, and Gly301 form hydrogen bonds with the hydroxyl groups of unit A. Glu45 and Tyr145 form hydrogen bonds with the hydroxyl groups of unit B. Asp193 and Gln197 form hydrogen bonds with the hydroxyl groups at unit C. These interactions are shared among the Sopn-bound structures. Contribution of interactions at unit C to complex stability
additional information
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the complex structures with substrates Sop3-5s bound can be overlaid well, molecular dynamics and three-dimensional structure modeling, architecture of the ligand-binding site, overview. Hydrogen bonds play a pivotal role in stabilizing the SO-BP-Sopn complexes. Thr95, Thr96, Glu147, and Gly301 form hydrogen bonds with the hydroxyl groups of unit A. Glu45 and Tyr145 form hydrogen bonds with the hydroxyl groups of unit B. Asp193 and Gln197 form hydrogen bonds with the hydroxyl groups at unit C. These interactions are shared among the Sopn-bound structures. Contribution of interactions at unit C to complex stability
Show AA Sequence and Transmembrane Helices (401 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme structure analysis and modeling, enzyme SO-BP is classified in structural cluster D-I of solute-binding proteins, SBPs. The complex structures with substrates Sop3-5s bound can be overlaid well
additional information
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enzyme structure analysis and modeling, enzyme SO-BP is classified in structural cluster D-I of solute-binding proteins, SBPs. The complex structures with substrates Sop3-5s bound can be overlaid well
additional information
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export of succinoglycan, components involved are encoded by exsA, function concluded from homologies to NdvA transporter
additional information
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ExpD1, function concluded from homologies to ABC transporters
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified SO-BP, comprisng residues 26-422 without the signal peptide, in a ligand-free form and in complexes with substrates Sop3, Sop4, and Sop5, X-ray diffraction structure determination and analysis at 1.6-2.2 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
energetic contributions of interactions at unit C to the binding to SO-BP, mo,ecular dynamics, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fath, M.J.; Kolter, R.
ABC transporters: bacterial exporters
Microbiol. Rev.
57
995-1017
1993
Agrobacterium tumefaciens, Sinorhizobium meliloti
brenda
Becker, A.; Kuster, H.; Niehaus, K.; Puhler, A.
Extension of the Rhizobium meliloti succinoglycan biosynthesis gene cluster identification of the exsA gene encoding an ABC transporter protein, and the exsB gene which probably codes for a regulator of succinoglycan biosynthesis
Mol. Gen. Genet.
249
487-497
1995
Sinorhizobium meliloti
brenda
Becker, A.; Ruberg, S.; Kuster, H.; Roxlau, A.A.; Keller, M.; Ivashina, T.; Cheng, H.P.; Walker, G.C.; Puhler, A.
The 32-kilobase exp gene cluster of Rhizobium meliloti directing the biosynthesis of galactoglucan genetic organization and properties of the encoded gene products
J. Bacteriol.
179
1375-1384
1997
Sinorhizobium meliloti
brenda
Beauvais, A.; Bruneau, J.M.; Mol, P.C.; Buitrago, M.J.; Legrand, R.; Latge, J.P.
Glucan synthase complex of Aspergillus fumigatus
J. Bacteriol.
183
2273-2279
2001
Aspergillus fumigatus
brenda
Abe, K.; Sunagawa, N.; Terada, T.; Takahashi, Y.; Arakawa, T.; Igarashi, K.; Samejima, M.; Nakai, H.; Taguchi, H.; Nakajima, M.; Fushinobu, S.
Structural and thermodynamic insights into -1,2-glucooligosaccharide capture by a solute-binding protein in Listeria innocua
J. Biol. Chem.
293
8812-8828
2018
Listeria innocua (Q92AS8), Listeria innocua
brenda
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EXTERNAL LINKS (specific for EC-Number 7.5.2.3)
Transporter Classification Database (TCDB): 3.A.1.108.1
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Release 2023.1 (January 2023)
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