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Information on EC 2.1.2.2 - phosphoribosylglycinamide formyltransferase 1 and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC2.1.2.2

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IUBMB Comments

Two enzymes are known to catalyse the third step in de novo purine biosynthesis. This enzyme utilizes 10-formyltetrahydrofolate as the formyl donor, while the other enzyme, EC 6.3.1.21, phosphoribosylglycinamide formyltransferase 2, utilizes formate. In vertebrates this activity is catalysed by a trifunctional enzyme that also catalyses the activities of EC 6.3.4.13, phosphoribosylamine—glycine ligase and EC 6.3.3.1, phosphoribosylformylglycinamidine cyclo-ligase.

The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms

Synonyms
glycinamide ribonucleotide formyltransferase, glycinamide ribonucleotide transformylase, garft, gar tfase, gar transformylase, garftase, phosphoribosylglycinamide formyltransferase, glycinamide ribonucleotide formyl transferase, gar formyltransferase, gartfase, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-amino-N-ribosylacetamide 5'-phosphate transformylase
-
-
-
-
5'-phosphoribosylglycinamide transformylase
-
-
-
-
5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase
-
-
-
-
ADE8
-
-
-
-
GAR formyltransferase
-
-
-
-
GAR TFase
-
-
-
-
GAR transformylase
-
-
-
-
GART
-
-
-
-
glycinamide ribonucleotide transformylase
-
-
-
-
PurN
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
MetaCyc
5-aminoimidazole ribonucleotide biosynthesis I, tetrahydrofolate salvage from 5,10-methenyltetrahydrofolate
SYSTEMATIC NAME
IUBMB Comments
10-formyltetrahydrofolate:5'-phosphoribosylglycinamide N-formyltransferase
Two enzymes are known to catalyse the third step in de novo purine biosynthesis. This enzyme utilizes 10-formyltetrahydrofolate as the formyl donor, while the other enzyme, EC 6.3.1.21, phosphoribosylglycinamide formyltransferase 2, utilizes formate. In vertebrates this activity is catalysed by a trifunctional enzyme that also catalyses the activities of EC 6.3.4.13, phosphoribosylamine---glycine ligase and EC 6.3.3.1, phosphoribosylformylglycinamidine cyclo-ligase.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-02-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
show the reaction diagram
10-formyltetrahydrofolate + N5-hydroxyornithine
tetrahydrofolate + N5-formyl-N5-hydroxyornithine
show the reaction diagram
-
Substrates: -
Products: -
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
show the reaction diagram
-
Substrates: involved in pyoverdine synthesis
Products: -
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
expression regulated by amount of iron in the growth medium
top print hide Go to Organism Search
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A071L5M9_PSEAI
222
0
24747
TrEMBL
-
A0A0C7D3G1_PSEAI
222
0
24734
TrEMBL
-
A0A0F6UG69_PSEAI
222
0
24733
TrEMBL
-
A0A3M5DLL2_PSEAI
291
0
33153
TrEMBL
-
A0A3M5EIG0_PSEAI
76
0
7568
TrEMBL
Secretory Pathway (Reliability: 2)
A0A509JRP0_PSEAI
275
0
31053
TrEMBL
-
A0A6A9K892_PSEAI
222
0
24747
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6B0QLE7_PSEAI
275
0
31300
TrEMBL
Secretory Pathway (Reliability: 1)
A0AAQ3R4E4_PSEAI
275
0
31301
TrEMBL
-
A0ABD7JWU7_PSEAI
275
0
31347
TrEMBL
-
A0ABD7K0V7_PSEAI
222
0
24711
TrEMBL
Secretory Pathway (Reliability: 1)
P72114_PSEAI
275
0
31017
TrEMBL
other Location (Reliability: 5)
Q5DIT2_PSEAI
275
0
31067
TrEMBL
-
Q5DIP8_PSEAI
252
0
28729
TrEMBL
Mitochondrion (Reliability: 3)
Q5DIW2_PSEAI
275
0
31039
TrEMBL
-
Q8G958_PSEAI
275
0
31329
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30985
-
x * 30985, calculated
31000
-
DNA sequencing
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 30985, calculated
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme disruption mutant, no synthesis of pyoverdine, mutant strain is unable to grow on King´s B agar containing iron-chelating agent EDTA
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
pvdF gene characterization
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McMorran, B.J.; Kumara, H.M.C.S.; Sullivan, K.; Lamont, I.L.
Involvement of a transformylase enzyme in siderophore synthesis in Pseudomonas aeruginosa
Microbiology
147
1517-1524
2001
Escherichia coli, Saccharomyces cerevisiae, Bacillus subtilis, Drosophila melanogaster, Pseudomonas aeruginosa, Arabidopsis thaliana
Manually annotated by BRENDA team