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cyoA cyoA folK-2 folK-2 folK-1 folK-1 AAO53960.1 AAO53960.1 AAO53799.1 AAO53799.1 cycB cycB sdhA sdhA sdhC sdhC nuoM nuoM nuoL nuoL nouK nouK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoB nuoB nuoE nuoE nuoA nuoA AAO56346.1 AAO56346.1 AAO56028.1 AAO56028.1 sdhB sdhB ccoN ccoN ccoO ccoO ccoP ccoP cyoB cyoB
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Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
cyoACytochrome o ubiquinol oxidase, subunit II; See PMID:20190049 for expression data. (313 aa)
folK-22-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; See PMID:20190049 for expression data; similar to GP:3970811, and SP:P26281; identified by sequence similarity; putative. (168 aa)
folK-12-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase. (174 aa)
AAO53960.1Ferredoxin; Similar to GP:1518927, GB:M23219, SP:P17583, PID:145644, GB:U00096, PID:1657537, and PID:1786536; identified by sequence similarity; putative. (83 aa)
AAO53799.1Conserved hypothetical protein; Identified by Glimmer2; putative. (103 aa)
cycBCytochrome c5; See PMID:20190049 for expression data; similar to GB:Z11766, and PID:47029; identified by sequence similarity; putative. (107 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Similar to SP:P10444, GB:D12485, GB:M57736, SP:P22413, PID:189650, PID:219944, and PID:219945; identified by sequence similarity; putative; see PMID:20190049 for expression data; similar to SP:P10444, GB:D12485, GB:M57736, SP:P22413, PID:189650, PID:219944, and PID:219945, identified by sequence similarity, putative; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (590 aa)
sdhCSuccinate dehydrogenase, cytochrome b556 subunit; See PMID:20190049 for expression data; similar to GP:9947544, and SP:P10446; identified by sequence similarity; putative. (124 aa)
nuoMNADH dehydrogenase I, M subunit; See PMID:20190049 for expression data. (510 aa)
nuoLNADH dehydrogenase I, L subunit; This gene assignment is based in part on its location in a gene cluster; see PMID:20190049 for expression data; similar to SP:P50939; identified by sequence similarity; putative. (617 aa)
nouKNADH dehydrogenase I, K subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (102 aa)
nuoJNADH dehydrogenase I, J subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (169 aa)
nuoINADH dehydrogenase I, I subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (182 aa)
nuoHNADH dehydrogenase I, H subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (335 aa)
nuoGNADH dehydrogenase I, G subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). (905 aa)
nuoFNADH dehydrogenase I, F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (452 aa)
nuoBNADH dehydrogenase I, B subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (224 aa)
nuoENADH dehydrogenase I, E subunit; See PMID:20190049 for expression data. (165 aa)
nuoANADH dehydrogenase I, A subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (137 aa)
AAO56346.1Cytochrome c family protein; See PMID:20190049 for expression data; identified by match to PFAM protein family HMM PF00034. (95 aa)
AAO56028.1Conserved hypothetical protein; Similar to SP:O87386; identified by sequence similarity; putative. (96 aa)
sdhBSuccinate dehydrogenase, iron-sulfur protein; Similar to SP:P07014, GB:L05004, and PID:152957; identified by sequence similarity; putative; see PMID:20190049 for expression data; similar to SP:P07014, GB:L05004, and PID:152957, identified by sequence similarity, putative. (234 aa)
ccoNCytochrome c oxidase, cbb3-type, subunit I; Identified by match to PFAM protein family HMM PF00115; Belongs to the heme-copper respiratory oxidase family. (480 aa)
ccoOCytochrome c oxidase, cbb3-type, subunit II; See PMID:20190049 for expression data; identified by match to PFAM protein family HMM PF02433. (202 aa)
ccoPCytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (325 aa)
cyoBCytochrome o ubiquinol oxidase, subunit I; See PMID:20190049 for expression data; Belongs to the heme-copper respiratory oxidase family. (670 aa)
Your Current Organism:
Pseudomonas syringae tomato
NCBI taxonomy Id: 223283
Other names: P. syringae pv. tomato str. DC3000, Pseudomonas syringae DC3000, Pseudomonas syringae pv. tomato DC3000, Pseudomonas syringae pv. tomato str. ATCC BAA-871, Pseudomonas syringae pv. tomato str. DC3000
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