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EC Tree
IUBMB Comments Catalyses the guanylation of the molybdenum cofactor. This modification occurs only in prokaryotes.
The enzyme appears in viruses and cellular organisms
Synonyms
protein fa,
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MobA
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GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor
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nucleotidyl group transfer
nucleotidyl group transfer
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nucleotidyl group transfer
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nucleotidyl group transfer
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GTP:molybdenum cofactor guanylyltransferase
Catalyses the guanylation of the molybdenum cofactor. This modification occurs only in prokaryotes.
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GTP + molybdenum cofactor
diphosphate + guanylyl molybdenum cofactor
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?
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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-
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?
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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?
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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?
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GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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?
GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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GTP + MoO2(OH)Dtpp-mP
diphosphate + MoO2(OH)Dtpp-mGDP
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0.0065
GTP
pH 7.2, temperature not specified in the publication, wild-type
0.0455
GTP
pH 7.2, temperature not specified in the publication, mutant L12T/G14A/P79L/A81T/G82S
0.0489
GTP
pH 7.2, temperature not specified in the publication, mutant L12T/G14A
0.0706
GTP
pH 7.2, temperature not specified in the publication, mutant P79L/A81T/G82S
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0.0016
GTP
pH 7.2, temperature not specified in the publication, mutant L12T/G14A/P79L/A81T/G82S
0.0041
GTP
pH 7.2, temperature not specified in the publication, mutant P79L/A81T/G82S
0.0048
GTP
pH 7.2, temperature not specified in the publication, wild-type
0.0053
GTP
pH 7.2, temperature not specified in the publication, mutant L12T/G14A
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UniProt
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SwissProt
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K-12
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brenda
K-12
SwissProt
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metabolism
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molybdenum cofactor biosynthesis
metabolism
molybdenum cofactor biosynthesis
metabolism
molybdenum cofactor biosynthesis
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Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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PDB 1FR9 and PDB 1FRW (complex with Mn-GTP)
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L12T/G14A
Km (GTP) increased compared to wild-type, kcat slightly increased compared to wild-type, mutant shows 11-19 fold increased KD (GTP) dissociation constant compared to wild-type
L12T/G14A/P79L/A81T/G82S
Km (GTP) 7-10fold increased compared to wild-type, kcat 3fold decreased compared to wild-type,mutant shows 11-19 fold increased KD (GTP) dissociation constant compared to wild-type
N180D/N182D
wild type activity
P79L/A81T/G82S
Km (GTP) increased compared to wild-type, kcat slightly decreased compared to wild-type, mutant shows 11-19 fold increased KD (GTP) dissociation constant compared to wild-type
additional information
hybrid protein consisting of N-terminal MobA protein and C-terminal MocA protein shows similar Km (GTP) compared to wild-type, and increased kcat compared to wild-type, mutant shows comparable KD (GTP) dissociation constant compared to wild-type. Compared to wild-type Apo-TorA and TorD only interact with hybrid proteins that contain the C terminus of MobA, but no interaction is identified with variants containing the C terminus of MocA
additional information
hybrid protein consisting of N-terminal MocA protein and C-terminal MobA protein does not show any reactivity towards substrate GTP. Compared to wild-type Apo-TorA and TorD only interact with hybrid proteins that contain the C terminus of MobA, but no interaction is identified with variants containing the C terminus of MocA
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DEAE cellulose column, Cibacron blue affinity column, Superose-12 gel filtration column
nickel-nitrilotriacetic acid column
using Ni-NTA chromatography
DEAE cellulose column, Cibacron blue affinity column, Superose-12 gel filtration column
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DEAE cellulose column, Cibacron blue affinity column, Superose-12 gel filtration column
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expressed in Escherichia coli as a His-tagged fusion protein
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Temple, C.A.; Rajagopalan, K.V.
Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase
J. Biol. Chem.
275
40202-40210
2000
Rhodobacter sphaeroides (P95645)
brenda
Lake, M.W.; Temple, C.A.; Rajagopalan, K.V.; Schindelin, H.
The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis
J. Biol. Chem.
275
40211-40217
2000
Escherichia coli
brenda
Guse, A.; Stevenson, C.E.; Kuper, J.; Buchanan, G.; Schwarz, G.; Giordano, G.; Magalon, A.; Mendel, R.R.; Lawson, D.M.; Palmer, T.
Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA
J. Biol. Chem.
278
25302-25307
2003
Escherichia coli (P32173)
brenda
Neumann, M.; Seduk, F.; Iobbi-Nivol, C.; Leimkuhler, S.
Molybdopterin dinucleotide biosynthesis in Escherichia coli: Identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides
J. Biol. Chem.
286
1400-1408
2011
Escherichia coli (P32173)
brenda
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2.7.7.77 molybdenum cofactor guanylyltransferase
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