hemO protein (Pseudomonas putida KT2440) - STRING interaction network

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Predicted Interactions

gene neighborhood

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[Homology]

Score

hemO

Heme oxygenase. (197 aa)

Predicted Functional Partners:

PP_2582

0.914

bfr-I

0.901

bfr-II

0.901

PP_4856

0.901

cyoE1

0.900

hemH

0.900

cyoE

0.900

PP_1006

0.793

fecA

0.782

fecI

0.756

Your Current Organism:

Pseudomonas putida KT2440

NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
PP_1006	PP_2582	PP_1006	PP_2582	Putative outer membrane heme receptor; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component; Transport and binding proteins.	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.485
PP_1006	fecI	PP_1006	PP_3577	Putative outer membrane heme receptor; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component; Transport and binding proteins.	RNA polymerase, sigma 19 factor; Function of homologous gene experimentally demonstrated in an other organism; regulator; Transcription; Belongs to the sigma-70 factor family. ECF subfamily.	0.646
PP_1006	hemO	PP_1006	PP_1005	Putative outer membrane heme receptor; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component; Transport and binding proteins.	Heme oxygenase.	0.793
PP_2582	PP_1006	PP_2582	PP_1006	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Putative outer membrane heme receptor; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative membrane component; Transport and binding proteins.	0.485
PP_2582	PP_4856	PP_2582	PP_4856	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Ferritin, Dps family protein.	0.901
PP_2582	bfr-I	PP_2582	PP_0482	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.902
PP_2582	bfr-II	PP_2582	PP_1082	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.901
PP_2582	cyoE	PP_2582	PP_0816	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.	0.900
PP_2582	cyoE1	PP_2582	PP_0110	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	CyoE like protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.	0.900
PP_2582	hemH	PP_2582	PP_0744	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.	0.900
PP_2582	hemO	PP_2582	PP_1005	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Heme oxygenase.	0.914
PP_4856	PP_2582	PP_4856	PP_2582	Ferritin, Dps family protein.	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.901
PP_4856	bfr-I	PP_4856	PP_0482	Ferritin, Dps family protein.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.931
PP_4856	bfr-II	PP_4856	PP_1082	Ferritin, Dps family protein.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.941
PP_4856	hemH	PP_4856	PP_0744	Ferritin, Dps family protein.	Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.	0.912
PP_4856	hemO	PP_4856	PP_1005	Ferritin, Dps family protein.	Heme oxygenase.	0.901
bfr-I	PP_2582	PP_0482	PP_2582	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Putative Heme oxygenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.902
bfr-I	PP_4856	PP_0482	PP_4856	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Ferritin, Dps family protein.	0.931
bfr-I	bfr-II	PP_0482	PP_1082	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	0.909
bfr-I	hemH	PP_0482	PP_0744	Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.	Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.	0.914