tyrA protein (Synechococcus sp. WH 8102) - STRING interaction network

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Score

tyrA

Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. (127 aa)

Predicted Functional Partners:

aroC

0.946

pheA

0.925

trpE

0.904

sppA

0.842

pabA

0.822

SYNW2432

0.809

menF

0.800

SYNW2384

0.800

SYNW1775

0.717

SYNW2058

0.674

Your Current Organism:

Synechococcus sp. WH 8102

NCBI taxonomy Id: 84588
Other names: S. sp. WH 8102, Synechococcus sp. WH8102

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
SYNW1775	tyrA	SYNW1775	SYNW1885	Putative divalent cation tolerance protein.	Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.	0.717
SYNW2058	SYNW2384	SYNW2058	SYNW2384	Prephenate dehydrogenase; Putative assignment.	Conserved hypothetical protein.	0.815
SYNW2058	aroC	SYNW2058	SYNW0308	Prephenate dehydrogenase; Putative assignment.	Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	0.811
SYNW2058	menF	SYNW2058	SYNW2308	Prephenate dehydrogenase; Putative assignment.	Isochorismate synthase.	0.834
SYNW2058	pheA	SYNW2058	SYNW2142	Prephenate dehydrogenase; Putative assignment.	Chorismate mutase-Prephenate dehydratase; Putative assignment.	0.965
SYNW2058	tyrA	SYNW2058	SYNW1885	Prephenate dehydrogenase; Putative assignment.	Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.	0.674
SYNW2384	SYNW2058	SYNW2384	SYNW2058	Conserved hypothetical protein.	Prephenate dehydrogenase; Putative assignment.	0.815
SYNW2384	aroC	SYNW2384	SYNW0308	Conserved hypothetical protein.	Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	0.800
SYNW2384	menF	SYNW2384	SYNW2308	Conserved hypothetical protein.	Isochorismate synthase.	0.908
SYNW2384	trpE	SYNW2384	SYNW2045	Conserved hypothetical protein.	Anthranilate synthase component I and chorismate binding enzyme.	0.815
SYNW2384	tyrA	SYNW2384	SYNW1885	Conserved hypothetical protein.	Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.	0.800
SYNW2432	aroC	SYNW2432	SYNW0308	Possible p-aminobenzoate synthetase; Citation: Goncharoff and Nichols (1984) J. Bacteriol. 159:57-62.	Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	0.897
SYNW2432	pabA	SYNW2432	SYNW2315	Possible p-aminobenzoate synthetase; Citation: Goncharoff and Nichols (1984) J. Bacteriol. 159:57-62.	Para-aminobenzoate synthase component II; CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN; Citation: Kaplan and Nichols (1983) J. Mol. Biol. 168:451-468; Tran et al. (1990) J. Bacteriol. 172:397-410.	0.999
SYNW2432	trpE	SYNW2432	SYNW2045	Possible p-aminobenzoate synthetase; Citation: Goncharoff and Nichols (1984) J. Bacteriol. 159:57-62.	Anthranilate synthase component I and chorismate binding enzyme.	0.838
SYNW2432	tyrA	SYNW2432	SYNW1885	Possible p-aminobenzoate synthetase; Citation: Goncharoff and Nichols (1984) J. Bacteriol. 159:57-62.	Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.	0.809
aroC	SYNW2058	SYNW0308	SYNW2058	Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	Prephenate dehydrogenase; Putative assignment.	0.811
aroC	SYNW2384	SYNW0308	SYNW2384	Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	Conserved hypothetical protein.	0.800
aroC	SYNW2432	SYNW0308	SYNW2432	Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	Possible p-aminobenzoate synthetase; Citation: Goncharoff and Nichols (1984) J. Bacteriol. 159:57-62.	0.897
aroC	menF	SYNW0308	SYNW2308	Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	Isochorismate synthase.	0.872
aroC	pabA	SYNW0308	SYNW2315	Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	Para-aminobenzoate synthase component II; CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN; Citation: Kaplan and Nichols (1983) J. Mol. Biol. 168:451-468; Tran et al. (1990) J. Bacteriol. 172:397-410.	0.887