Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 7.6.2.10 - ABC-type glycerol 3-phosphate transporter

for references in articles please use BRENDA:EC7.6.2.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB 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. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of glycerol 3-phosphate and various glycerophosphodiesters.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q5SLB4
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
+
sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
=
+
+
+
[glycerol 3-phosphate-binding protein][side 1]
Synonyms
glycerol-3-phosphate transporter, glpt transporter, glycerol 3-phosphate transporter, ugpabce transporter, sn-glycerol-3-phosphate-binding periplasmic protein, ugpabce, sn-glycerol-3-phosphate transporter, g3p transporter, glycerol-3-phosphate permease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycerol-3-phosphate-transporting ATPase
-
-
-
-
sn-glycerol-3-phosphate transport system permease protein upgA
-
-
-
-
sn-glycerol-3-phosphate transport system permease protein upgE
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transmembrane transport
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, sn-glycerol 3-phosphate-importing)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. A bacterial enzyme that interacts with an extracytoplasmic substrate binding protein and mediates the high affinity uptake of glycerol 3-phosphate and various glycerophosphodiesters.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
show the reaction diagram
-
-
-
?
additional information
?
-
the Thermus thermophilus UgpB also transports glycerophosphocholine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + sn-glycerol 3-phosphate-[glycerol 3-phosphate-binding protein][side 1]
ADP + phosphate + sn-glycerol 3-phosphate[side 2] + [glycerol 3-phosphate-binding protein][side 1]
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
Thermus thermophilus (TtUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview. The random clustering of the proteins clearly suggests that, at least, based on sequence homology of proteins no fundamental distinction can be made between Sec- and Tat-specific UgpB proteins. This is indicative of the plausible inference that the targeting of UgpB proteins to Tat or Sec pathway solely depends upon the characteristics of the signal peptide sequence rather than the whole protein
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
conservation of the signature residues of UgpB proteins, Sec- and Tat-specific signal peptides vary in their length because of different properties associated with them, Sec-predicted UgpB proteins contain a shorter signal peptide compared to Tat-specific, overview. The majority of UgpB proteins have Sec-specific tripartite structure in their signal peptide. Sec-predicted UgpB proteins contain highly hydrophobic h-region of the tripartite structure
physiological function
periplasmic UgpB protein is a periplasmic solute (or substrate) binding protein of UgpABCE ATP-binding cassette (ABC) transporter, which mediates the sequestration of either sn-glycerol-3-phosphate (G3P) or glycerophosphocholine (GPC) molecules in the periplasmic space. UgpB protein from Thermus thermophilus (TtUgpB) follows the Sec pathway for its translocation to the periplasm during its pathogenesis, probable mode of translocation of UgpB proteins in the plasma membrane via the Tat pathway and the Sec pathway, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q5SLB4_THET8
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
417
0
45290
TrEMBL
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
UgpB proteins contain a conserved signal peptidase cleavage site irrespective of their translocation pathway
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ugpB, sequence comparisons and phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Adhikari, R.; Singh, D.; Chandravanshi, M.; Dutta, A.; Kanaujia, S.
UgpB, a periplasmic component of the UgpABCE ATP-binding cassette transporter, predominantly follows the Sec translocation pathway
Meta Gene
13
129-139
2017
Mycobacterium tuberculosis (A5U6I5), Escherichia coli (P0AG80), Thermus thermophilus (Q5SLB4), Thermus thermophilus DSM 579 (Q5SLB4), Mycobacterium tuberculosis ATCC 25177 (A5U6I5), Thermus thermophilus ATCC 27634 (Q5SLB4)
-
Manually annotated by BRENDA team