STRINGSTRING
AGG87268.1 AGG87268.1 AGG87389.1 AGG87389.1 AGG87390.1 AGG87390.1 AGG87392.1 AGG87392.1 AGG87451.1 AGG87451.1 AGG87452.1 AGG87452.1 AGG88165.1 AGG88165.1 AGG88442.1 AGG88442.1 nuoB nuoB AGG88609.1 AGG88609.1 AGG88610.1 AGG88610.1 AGG88611.1 AGG88611.1 nuoH nuoH nuoI nuoI AGG88614.1 AGG88614.1 AGG88616.1 AGG88616.1 AGG88617.1 AGG88617.1 AGG88824.1 AGG88824.1 AGG88825.1 AGG88825.1 AGG88826.1 AGG88826.1 AGG88961.1 AGG88961.1 AGG88962.1 AGG88962.1 AGG89296.1 AGG89296.1 AGG89297.1 AGG89297.1 AGG89299.1 AGG89299.1 AGG89396.1 AGG89396.1 AGG89470.1 AGG89470.1 AGG89471.1 AGG89471.1 AGG89473.1 AGG89473.1 AGG89571.1 AGG89571.1 AGG89572.1 AGG89572.1 AGG89678.1 AGG89678.1 AGG89758.1 AGG89758.1 AGG89950.1 AGG89950.1 AGG89951.1 AGG89951.1 AGG89957.1 AGG89957.1 AGG89994.1 AGG89994.1 AGG90016.1 AGG90016.1 AGG90017.1 AGG90017.1 AGG90101.1 AGG90101.1 AGG90501.1 AGG90501.1 AGG90704.1 AGG90704.1 AGG90767.1 AGG90767.1 AGG90806.1 AGG90806.1
Nodes:
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.
Node Color
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:
AGG87268.1Cytochrome c, mono- and diheme variants family; PFAM: Cytochrome c. (463 aa)
AGG87389.1TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa)
AGG87390.1PFAM: domain; FAD binding domain; TIGRFAM: succinate dehydrogenase, flavoprotein subunit, E. coli/mitochondrial subgroup; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (598 aa)
AGG87392.1PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit. (141 aa)
AGG87451.1Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (303 aa)
AGG87452.1Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (538 aa)
AGG88165.1Cytochrome c, mono- and diheme variants family; PFAM: Cytochrome c. (429 aa)
AGG88442.1Ketosteroid isomerase-like enzyme. (357 aa)
nuoBNADH dehydrogenase subunit B; 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. (185 aa)
AGG88609.1PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit; TIGRFAM: NADH-quinone oxidoreductase, E subunit. (189 aa)
AGG88610.1NADH dehydrogenase subunit F; 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. (436 aa)
AGG88611.1NADH dehydrogenase subunit G; 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. Belongs to the complex I 75 kDa subunit family. (779 aa)
nuoHNADH:ubiquinone oxidoreductase subunit 1 (chain H); 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. (342 aa)
nuoINADH dehydrogenase subunit I; 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. (163 aa)
AGG88614.1NADH:ubiquinone oxidoreductase subunit 6 (chain J); 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. (214 aa)
AGG88616.1PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L. (681 aa)
AGG88617.1PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (502 aa)
AGG88824.1Cbb3-type cytochrome oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit I; cytochrome oxidase maturation protein, cbb3-type. (538 aa)
AGG88825.1PFAM: Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. (210 aa)
AGG88826.1Cytochrome c, mono- and diheme variants family; PFAM: Cytochrome c. (197 aa)
AGG88961.1PFAM: Cytochrome c. (106 aa)
AGG88962.1PFAM: Cytochrome c. (117 aa)
AGG89296.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family. (488 aa)
AGG89297.1PFAM: Cytochrome C oxidase, mono-heme subunit/FixO; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II. (220 aa)
AGG89299.1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (302 aa)
AGG89396.1Nitric oxide reductase large subunit; PFAM: Cytochrome C and Quinol oxidase polypeptide I. (765 aa)
AGG89470.1TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (260 aa)
AGG89471.1PFAM: domain; FAD binding domain; TIGRFAM: succinate dehydrogenase, flavoprotein subunit, E. coli/mitochondrial subgroup; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (595 aa)
AGG89473.1PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit. (131 aa)
AGG89571.1Heme/copper-type cytochrome/quinol oxidase, subunit 2; PFAM: Cytochrome C oxidase subunit II, periplasmic domain. (182 aa)
AGG89572.1Heme/copper-type cytochrome/quinol oxidase, subunit 1; PFAM: Cytochrome C and Quinol oxidase polypeptide I. (495 aa)
AGG89678.1PFAM: 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK); TIGRFAM: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase. (159 aa)
AGG89758.1PFAM: Cytochrome c. (268 aa)
AGG89950.1PFAM: Cytochrome c. (321 aa)
AGG89951.1Nitric oxide reductase large subunit; PFAM: Cytochrome C and Quinol oxidase polypeptide I. (565 aa)
AGG89957.1Nitric oxide reductase large subunit; PFAM: Cytochrome C and Quinol oxidase polypeptide I. (760 aa)
AGG89994.1Hypothetical protein. (417 aa)
AGG90016.1PFAM: Cytochrome C1 family. (252 aa)
AGG90017.1Cytochrome b subunit of the bc complex; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (433 aa)
AGG90101.1Hypothetical protein. (86 aa)
AGG90501.1PFAM: Cytochrome c. (102 aa)
AGG90704.1Cytochrome c, mono- and diheme variants family; PFAM: Cytochrome c. (427 aa)
AGG90767.1PFAM: 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK); TIGRFAM: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase. (162 aa)
AGG90806.1PFAM: Cytochrome c. (173 aa)
Your Current Organism:
Rhodanobacter denitrificans
NCBI taxonomy Id: 666685
Other names: DSM 23569, JCM 17641, R. denitrificans, Rhodanobacter denitrificans Prakash et al. 2012, Rhodanobacter sp. 116-2, Rhodanobacter sp. 2APBS1, Rhodanobacter sp. FW104-R3, strain 2APBS1
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