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Information on EC 2.7.1.206 - protein-Npi-phosphohistidine-L-sorbose phosphotransferase

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EC Tree
IUBMB Comments
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
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UNIPROT: Q9RGG2 not found.
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The enzyme appears in viruses and cellular organisms
Synonyms
l-sorbose pts, l-sorbose-specific enzyme ii, eiisor, eiicsor, eiidsor, eiiasor, eiibsor, sorfbam, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EC 2.7.1.69
-
-
formerly, part transferred
-
EIIASor
EIIBSor
EIICSor
EIIDSor
EIISor
-
-
-
-
L-sorbose PTS
-
-
L-sorbose PTS EII
L-sorbose PTS permease
-
-
-
-
L-sorbose-specific enzyme II
sor ABCD
sorABFM
-
-
-
-
sorFBAM
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[protein]-Npi-phospho-L-histidine + L-sorbose[side 1] = [protein]-L-histidine + L-sorbose 1-phosphate[side 2]
show the reaction diagram
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
protein-Npi-phospho-L-histidine:L-sorbose Npi-phosphotransferase
This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9 (phosphoenolpyruvate---protein phosphotransferase). Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[protein]-Npi-phospho-L-histidine + L-sorbose[side 1]
[protein]-L-histidine + L-sorbose 1-phosphate[side 2]
show the reaction diagram
additional information
?
-
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
[protein]-Npi-phospho-L-histidine + L-sorbose[side 1]
[protein]-L-histidine + L-sorbose 1-phosphate[side 2]
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
EIIASor and EEIBSor and EIICSor and EIIDSor
Q9RGG5; Q9RGG4; Q9RGG3; Q9RGG2
UniProt
Manually annotated by BRENDA team
EIIASor and EEIBSor and EIICSor and EIIDSor
Q9RGG5; Q9RGG4; Q9RGG3; Q9RGG2
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PTRB_KLEPN
164
0
18456
Swiss-Prot
-
PTRB_LACCA
164
0
18304
Swiss-Prot
-
A0A7U9RAH6_9FIRM
167
0
18221
TrEMBL
-
A0A5K1IMM3_9ACTN
157
0
16831
TrEMBL
-
A0A645BX96_9ZZZZ
154
0
17385
TrEMBL
other Location (Reliability: 2)
A0A645HDM6_9ZZZZ
158
0
17371
TrEMBL
Mitochondrion (Reliability: 5)
A0A857K283_PEDPE
158
0
17579
TrEMBL
-
A0A645DZA5_9ZZZZ
104
0
11636
TrEMBL
other Location (Reliability: 1)
A0A2R8BHH5_9RHOB
133
0
14104
TrEMBL
-
A0A8B6ISP1_9ENTR
135
0
14577
TrEMBL
-
A0A5K1JDW6_9ACTN
160
0
17668
TrEMBL
-
A0A857K1N6_PEDPE
164
0
18014
TrEMBL
-
A0A6N7BRT6_PEDPE
133
0
14733
TrEMBL
-
A0A2H6A6B7_9BACT
157
0
17435
TrEMBL
-
A0A5K1ICH5_9ACTN
160
0
17507
TrEMBL
-
A0A1S6IQR0_9LACT
167
0
18902
TrEMBL
-
A0A7U9NEB4_9FIRM
158
0
17767
TrEMBL
-
A0A8B6B7G0_ECOLX
127
0
13815
TrEMBL
-
A0A414FWC8_9ACTN
163
0
17811
TrEMBL
-
A0A5K1J7I2_9ACTN
160
0
17442
TrEMBL
-
A0A644WE65_9ZZZZ
156
0
17737
TrEMBL
other Location (Reliability: 5)
W8T4Y4_ECOLX
158
0
17578
TrEMBL
-
A0A645D9L8_9ZZZZ
161
0
17596
TrEMBL
other Location (Reliability: 3)
A0A4V1BX58_9GAMM
160
0
17874
TrEMBL
-
A0A414FW85_9ACTN
160
0
17687
TrEMBL
-
A0A2A7MDE8_9CLOT
158
0
17471
TrEMBL
-
A0A7U9NKP1_9FIRM
155
0
16916
TrEMBL
-
A0A5K1JEQ3_9ACTN
160
0
17598
TrEMBL
-
A0A5K1JGN3_9ACTN
190
0
20601
TrEMBL
-
A0A7U3F3M5_9ENTR
164
0
18509
TrEMBL
-
A0A5K1IHM3_9ACTN
160
0
17603
TrEMBL
-
A0A8A0RKB8_9FIRM
158
0
17619
TrEMBL
-
A0A645B9E4_9ZZZZ
158
0
17719
TrEMBL
other Location (Reliability: 4)
A0A644WXX9_9ZZZZ
167
0
18935
TrEMBL
other Location (Reliability: 2)
A0A7G3F5F8_ENTCL
142
0
15069
TrEMBL
-
A0A5D3I338_MOOTH
163
0
17876
TrEMBL
-
A0A7U9NC93_9FIRM
160
0
17818
TrEMBL
-
A0A165QN53_LACPN
140
0
15168
TrEMBL
-
A0A7U9WXD8_LACJH
164
0
18589
TrEMBL
-
A0A8F5C565_9BACI
100
0
10861
TrEMBL
-
A0A6P1Q5B2_9GAMM
156
0
17302
TrEMBL
-
A0A645A7E2_9ZZZZ
161
0
17668
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14500
-
x * 14500, domain EIIASor, SDS-PAGE
14509
-
x * 14509, domain EIIASor, calculated from amino acid sequence
14985
Q9RGG5; Q9RGG4; Q9RGG3; Q9RGG2
x * 14985, domain EIIASor, calculated from amino acid sequence
18304
Q9RGG5; Q9RGG4; Q9RGG3; Q9RGG2
x * 18304, domain EIIBSor, calculated from amino acid sequence
18457
-
x * 18457, domain EIIBSor, calculated from amino acid sequence
19000
-
x * 19000, domain EIIBSor, SDS-PAGE
25000
-
x * 25000, domain EIICSor, SDS-PAGE
27000
-
x * 27000, domain EIIDSor, SDS-PAGE
27876
-
x * 27876, domain EIICSor, calculated from amino acid sequence
29002
Q9RGG5; Q9RGG4; Q9RGG3; Q9RGG2
x * 29002, domain EIICSor, calculated from amino acid sequence
29370
-
x * 29370, domain EIIDSor, calculated from amino acid sequence
30788
Q9RGG5; Q9RGG4; Q9RGG3; Q9RGG2
x * 30788, domain EIIDSor, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yebra, M.; Veyrat, A.; Santos, M.; Perez-Martnez, G.
Genetics of L-sorbose transport and metabolism in Lactobacillus casei
J. Bacteriol.
182
155-163
2000
Lacticaseibacillus casei (Q9RGG5 and Q9RGG4 and Q9RGG3 and Q9RGG2), Lacticaseibacillus casei, Lacticaseibacillus casei ATCC 393 (Q9RGG5 and Q9RGG4 and Q9RGG3 and Q9RGG2)
Manually annotated by BRENDA team
Wehmeier, U.; Whrl, B.; Lengeler, J.
Molecular analysis of the phosphoenolpyruvate-dependent l-sorbose: phosphotransferase system from Klebsiella pneumoniae and of its multidomain structure
Mol. Gen. Genet.
246
610-618
1995
Klebsiella pneumoniae, Klebsiella pneumoniae KAY2026
Manually annotated by BRENDA team