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Information on EC 2.7.7.13 - mannose-1-phosphate guanylyltransferase and Organism(s) Pseudomonas aeruginosa

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EC Tree
IUBMB Comments
The bacterial enzyme can also use ITP and dGTP as donors.
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Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
gmppb, gdp-mannose pyrophosphorylase, vtc1-1, gdp-d-mannose pyrophosphorylase, gdp-mp, osvtc1-1, osvtc1-3, nspase, mannose-1-phosphate guanylyltransferase, gdp-man pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDP-mannose pyrophosphorylase
-
-
-
-
GTP-mannose 1-phosphate guanylyltransferase
-
-
-
-
GTP-mannose-1-phosphate guanylyltransferase
-
-
-
-
guanosine 5'-diphospho-D-mannose pyrophosphorylase
-
-
-
-
guanosine diphosphomannose pyrophosphorylase
-
-
-
-
guanosine triphosphate-mannose 1-phosphate guanylyltransferase
-
-
-
-
guanylyltransferase, mannose 1-phosphate
-
-
-
-
mannose 1-phosphate guanylyltransferase (guanosine triphosphate)
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP:alpha-D-mannose-1-phosphate guanylyltransferase
The bacterial enzyme can also use ITP and dGTP as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-24-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-mannose
show the reaction diagram
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
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
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
Mg2+ or Mn2+ required for activity
Mn2+
Mg2+ or Mn2+ required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0082 - 0.0205
alpha-D-mannose 1-phosphate
0.0142
GDPmannose
pH 7.0, 25°C
0.0295 - 0.041
GTP
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G5EFX6_PSEAI
481
0
53102
TrEMBL
-
A0A8G4CZP3_PSEAI
479
0
52537
TrEMBL
-
A0A8G2QFS0_PSEAI
481
0
53158
TrEMBL
-
A0A8G7DEB7_PSEAI
481
0
53112
TrEMBL
-
A0A8G4JS99_PSEAI
488
0
53444
TrEMBL
-
A0A8H0XBV1_PSEAI
479
0
52674
TrEMBL
-
A0A8G3EEK6_PSEAI
488
0
53544
TrEMBL
-
A0A8G6VEY0_PSEAI
479
0
52622
TrEMBL
-
A0A5F1BMZ2_PSEAI
479
0
52592
TrEMBL
-
A0A8G7GK25_PSEAI
479
0
52574
TrEMBL
-
A0A1J0J2H1_PSEAI
479
0
52594
TrEMBL
-
A0A8G3NX52_PSEAI
488
0
53532
TrEMBL
-
A0A8G2Q898_PSEAI
479
0
52594
TrEMBL
-
A0A0C7CUG0_PSEAI
479
0
52594
TrEMBL
-
A0A8G3YEH0_PSEAI
479
0
52546
TrEMBL
-
A0A0A8RFX6_PSEAI
479
0
52568
TrEMBL
-
A0A8G6UT76_PSEAI
481
0
53109
TrEMBL
-
A0A431XIU1_PSEAI
479
0
52488
TrEMBL
-
A0A8G4I1Z5_PSEAI
479
0
52584
TrEMBL
-
A0A8G6R9J9_PSEAI
479
0
52620
TrEMBL
-
A0A072ZQ19_PSEAI
481
0
53128
TrEMBL
-
A0A3M5EAD7_PSEAI
539
1
59357
TrEMBL
-
A0A8G4E139_PSEAI
488
0
53547
TrEMBL
-
A0A8G4G1B3_PSEAI
481
0
53136
TrEMBL
-
A0A8F9JKQ7_PSEAI
481
0
53100
TrEMBL
-
A0A2R3IQW6_PSEAI
479
0
52441
TrEMBL
-
A0A0C6EZR6_PSEAI
481
0
53137
TrEMBL
-
A0A8G2QCR8_PSEAI
488
0
53577
TrEMBL
-
A0A8G4M558_PSEAI
488
0
53575
TrEMBL
-
A0A8G7CXX2_PSEAI
479
0
52565
TrEMBL
-
A0A8G4FNI4_PSEAI
481
0
53094
TrEMBL
-
A0A8G5NSM2_PSEAI
479
0
52546
TrEMBL
-
A0A643EBD9_PSEAI
479
0
52585
TrEMBL
-
A0A231IDW1_PSEAI
479
0
52565
TrEMBL
-
A0A8G4LWA6_PSEAI
488
0
53490
TrEMBL
-
A0A233SN23_PSEAI
488
0
53588
TrEMBL
-
A0A8G4AIG2_PSEAI
481
0
53140
TrEMBL
-
A0A8G3ZMI2_PSEAI
481
0
53096
TrEMBL
-
A0A8G3Z657_PSEAI
488
0
53449
TrEMBL
-
A0A8G3P575_PSEAI
481
0
53100
TrEMBL
-
A0A8G7L8T8_PSEAI
479
0
52610
TrEMBL
-
A0A6A9KEA1_PSEAI
481
0
53086
TrEMBL
-
O87383_PSEAI
488
0
53626
TrEMBL
-
A0A7M2ZRH1_PSEAI
479
0
52564
TrEMBL
-
A0A8G6UKH5_PSEAI
481
0
53149
TrEMBL
-
A0A2I2CIK0_PSEAI
479
0
52584
TrEMBL
-
A0A8G6AAE8_PSEAI
481
0
53181
TrEMBL
-
A0A7M2ZU21_PSEAI
488
0
53497
TrEMBL
-
A0A8G3ZTQ3_PSEAI
479
0
52555
TrEMBL
-
A0A659BQR5_PSEAI
481
0
53156
TrEMBL
-
A0A8G2QMJ5_PSEAI
479
0
52580
TrEMBL
-
A0A0A8RRH4_PSEAI
488
0
53530
TrEMBL
-
A0A7M3AWH6_PSEAI
488
0
53542
TrEMBL
-
A0A8G3EDQ6_PSEAI
479
0
52610
TrEMBL
-
A0A8G4B3V6_PSEAI
479
0
52622
TrEMBL
-
A0A8G4P4X3_PSEAI
481
0
53142
TrEMBL
-
A0A2U2XLB4_PSEAI
488
0
53548
TrEMBL
-
O87266_PSEAI
479
0
52632
TrEMBL
-
A0A8G4HHX5_PSEAI
488
0
53496
TrEMBL
-
A0A8G2WUH9_PSEAI
488
0
53580
TrEMBL
-
A0A2R3IW98_PSEAI
488
0
53524
TrEMBL
-
A0A0C6EUL7_PSEAI
488
0
53516
TrEMBL
-
A0A8G6XG15_PSEAI
479
0
52624
TrEMBL
-
A0A8G2NK87_PSEAI
481
0
53128
TrEMBL
-
A0A367M0S3_PSEAI
331
0
36139
TrEMBL
-
A0A6B1YLP5_PSEAI
479
0
52584
TrEMBL
-
A0A8G3T2I4_PSEAI
488
0
53518
TrEMBL
-
A0A8G8EU93_PSEAI
488
0
53536
TrEMBL
-
A0A8G2RRP3_PSEAI
479
0
52580
TrEMBL
-
A0A8G6VC64_PSEAI
488
0
53504
TrEMBL
-
A0A485FQK9_PSEAI
505
0
55911
TrEMBL
-
A0A8G3WFE9_PSEAI
488
0
53586
TrEMBL
-
A0A5K1SD51_PSEAI
479
0
52624
TrEMBL
-
A0A5E5QUL3_PSEAI
488
0
53552
TrEMBL
-
A0A8G7N0X5_PSEAI
481
0
53130
TrEMBL
-
A0A8G5RS14_PSEAI
481
0
53158
TrEMBL
-
A0A8G3CQC2_PSEAI
488
0
53562
TrEMBL
-
A0A8G2VKI6_PSEAI
488
0
53573
TrEMBL
-
A0A8G7PUA2_PSEAI
479
0
52691
TrEMBL
-
A0A8G6B079_PSEAI
488
0
53578
TrEMBL
-
A0A367M4E1_PSEAI
481
0
53156
TrEMBL
-
A0A3S3XR53_PSEAI
479
0
52555
TrEMBL
-
A0A8G4GSB5_PSEAI
481
0
53162
TrEMBL
-
A0A3S0IYA6_PSEAI
481
0
53135
TrEMBL
-
A0A8G4NBW1_PSEAI
479
0
52551
TrEMBL
-
A0A8G2XU64_PSEAI
479
0
52564
TrEMBL
-
A0A8G1K7I9_PSEAI
479
0
52565
TrEMBL
-
A0A8F9K0W0_PSEAI
481
0
53151
TrEMBL
-
A0A8G3MYI6_PSEAI
488
0
53603
TrEMBL
-
A0A8B4ZES4_PSEAI
479
0
52594
TrEMBL
-
A0A8G6KD95_PSEAI
481
0
53204
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
gel filtration, phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is a bifunctional enzyme catalyzing both the phosphomannose isomerase, i.e. PIM, and guanosine 5'-diphospho-D-mannose pyrophosphorylase, i.e. GMP, reaction
56000
1 * 56000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 56000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K175E
approx. 9% of wild-type activity, 600fold increase in Km for mannose 1-phosphate
K175Q
approx. 40% of wild-type activity, 3200fold increase in Km for mannose 1-phosphate
K175R
470fold increase in mannose 1-phosphate Km value
K20Q
enzyme is unable to support alginate synthesis although it shows no significant differences in Vmax and Km as compared to wild-type
R19H
approx. 50% of wild-type activity, 8fold increase in Km for mannose 1-phosphate
R19K
approx. 50% of wild-type activity, 2 and 6fold increase in Km for mannose 1-phosphate and GTP, respectively
R19L
approx. 50% of wild-type activity, 5fold increase in Km for mannose 1-phosphate and GTP, respectively
S12A
approx. 44% of wild-type activity, 2 and 3fold decrease in Km for mannose 1-phosphate and GTP, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Biogel, Q-Sepharose, Sephacryl-200
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and several PMI-GMP mutants in algA mutant 8853
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
May, T.B.; Shinabarger, D.; Boyd, A.; Chakrabarty, A.M.
Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa
J. Biol. Chem.
269
4872-4877
1994
Pseudomonas aeruginosa (P07874)
Manually annotated by BRENDA team
Shinabarger, D.; Berry, A.; May, T.B.; Rothmel, R.; Fialho, A.; Chakrabarty, A.M.
Purification and characterization of phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa
J. Biol. Chem.
266
2080-2088
1991
Pseudomonas aeruginosa (P07874), Pseudomonas aeruginosa
Manually annotated by BRENDA team