CN09_07420 protein (Agrobacterium rhizogenes)

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CN09_07420

Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (166 aa)

Predicted Functional Partners:

CN09_10375

0.750

tgt

0.750

queA

0.745

CN09_03380

0.719

coaD

0.677

CN09_06305

0.659

CN09_07425

0.654

pgk

0.565

ispDF

0.552

fusA

0.537

Your Current Organism:

Agrobacterium rhizogenes

NCBI taxonomy Id: 359
Other names: A. rhizogenes, ATCC 11325, Agrobacterium biovar 2, Agrobacterium genomic group 10, Agrobacterium genomic species 10, Agrobacterium genomosp. 10, Agrobacterium rhizogenes, Agrobacterium rhizogenes (RI plasmid PRI1724), Agrobacterium rhizogenes (RI plasmid PRI8196), Agrobacterium rhizogenes (RI plasmid PRIA4B), CFBP 5520, CIP 104328, DSM 30148, ICMP 5794, IFO 13257, JCM 20919, LMG 150, NBRC 13257, NCPPB 2991, Rhizobium rhizogenes, Rhizobium sp. LMG 9509

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CN09_03380	CN09_06305	CN09_03380	CN09_06305	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	0.420
CN09_03380	CN09_07420	CN09_03380	CN09_07420	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides	0.719
CN09_03380	CN09_07425	CN09_03380	CN09_07425	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides	0.719
CN09_03380	CN09_10375	CN09_03380	CN09_10375	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family	0.999
CN09_03380	coaD	CN09_03380	CN09_07430	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4’- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate; Belongs to the bacterial CoaD family	0.999
CN09_03380	fusA	CN09_03380	CN09_08910	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome	0.899
CN09_03380	ispDF	CN09_03380	CN09_07765	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Bifunctional enzyme IspD/IspF; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl- D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF)	0.999
CN09_03380	pgk	CN09_03380	CN09_02190	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Phosphoglycerate kinase; Converts 3-phospho-D-glycerate to 3-phospho-D-glyceroyl phosphate during the glycolysis pathway; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the phosphoglycerate kinase family	0.984
CN09_03380	tgt	CN09_03380	CN09_07410	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1’ of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1’ of the ribose to form th [...]	0.502
CN09_06305	CN09_03380	CN09_06305	CN09_03380	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	0.420
CN09_06305	CN09_07420	CN09_06305	CN09_07420	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides	0.659
CN09_06305	CN09_07425	CN09_06305	CN09_07425	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides	0.659
CN09_06305	CN09_10375	CN09_06305	CN09_10375	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family	0.999
CN09_06305	coaD	CN09_06305	CN09_07430	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4’- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate; Belongs to the bacterial CoaD family	0.798
CN09_06305	ispDF	CN09_06305	CN09_07765	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	Bifunctional enzyme IspD/IspF; Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl- D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF)	0.999
CN09_06305	queA	CN09_06305	CN09_07415	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	S-adenosylmethionine-tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA)	0.840
CN09_06305	tgt	CN09_06305	CN09_07410	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	Queuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1’ of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1’ of the ribose to form th [...]	0.584
CN09_07420	CN09_03380	CN09_07420	CN09_03380	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides	2-oxoisovalerate dehydrogenase; Derived by automated computational analysis using gene prediction method- Protein Homology	0.719
CN09_07420	CN09_06305	CN09_07420	CN09_06305	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides	Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source	0.659
CN09_07420	CN09_07425	CN09_07420	CN09_07425	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides	Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides	0.654

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