STRINGSTRING
EAQ10570.1 EAQ10570.1 EAQ11612.1 EAQ11612.1 EAQ11427.1 EAQ11427.1 EAQ11647.1 EAQ11647.1 EAQ11649.1 EAQ11649.1 EAQ11651.1 EAQ11651.1 EAQ11373.1 EAQ11373.1 EAQ11374.1 EAQ11374.1 EAQ11401.1 EAQ11401.1 EAQ15052.1 EAQ15052.1 apt apt EAQ14964.1 EAQ14964.1 EAQ14733.1 EAQ14733.1 EAQ14440.1 EAQ14440.1 EAQ14438.1 EAQ14438.1 EAQ14437.1 EAQ14437.1 EAQ14237.1 EAQ14237.1 EAQ12657.1 EAQ12657.1 EAQ12504.1 EAQ12504.1 EAQ12503.1 EAQ12503.1 EAQ13948.1 EAQ13948.1 EAQ13947.1 EAQ13947.1 EAQ13937.1 EAQ13937.1 EAQ13934.1 EAQ13934.1 EAQ13400.1 EAQ13400.1 EAQ13399.1 EAQ13399.1 EAQ13397.1 EAQ13397.1 EAQ13305.1 EAQ13305.1 EAQ13302.1 EAQ13302.1 EAQ13255.1 EAQ13255.1 EAQ12203.1 EAQ12203.1 EAQ12202.1 EAQ12202.1 EAQ12176.1 EAQ12176.1 EAQ11976.1 EAQ11976.1 EAQ12741.1 EAQ12741.1 EAQ10741.1 EAQ10741.1 EAQ11434.1 EAQ11434.1 EAQ11433.1 EAQ11433.1 nuoB nuoB EAQ12095.1 EAQ12095.1 EAQ12099.1 EAQ12099.1 nuoI nuoI nuoK nuoK
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:
EAQ10570.1Hypothetical protein; COG2010 Cytochrome c, mono- and diheme variants. (132 aa)
EAQ11612.1COG2010 Cytochrome c, mono- and diheme variants. (295 aa)
EAQ11427.1COG2010 Cytochrome c, mono- and diheme variants. (155 aa)
EAQ11647.1COG2010 Cytochrome c, mono- and diheme variants. (152 aa)
EAQ11649.1COG2010 Cytochrome c, mono- and diheme variants. (305 aa)
EAQ11651.1COG2010 Cytochrome c, mono- and diheme variants. (160 aa)
EAQ11373.1Putative 3-oxosteroid 1-dehydrogenase; COG1053 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit. (585 aa)
EAQ11374.1COG1053 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit. (569 aa)
EAQ11401.13-ketosteroid-1-dehydrogenase; COG1053 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit. (526 aa)
EAQ15052.1NADH-ubiquinone oxidoreductase family protein. (103 aa)
aptAdenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. (176 aa)
EAQ14964.13-ketosteroid-delta-1-dehydrogenase; COG1053 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit. (559 aa)
EAQ14733.1Hypothetical protein; COG2010 Cytochrome c, mono- and diheme variants. (131 aa)
EAQ14440.1COG2009 Succinate dehydrogenase/fumarate reductase, cytochrome b subunit. (127 aa)
EAQ14438.1COG1053 Succinate dehydrogenase/fumarate reductase, flavoprotein subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (601 aa)
EAQ14437.1COG0479 Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa)
EAQ14237.12-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; COG0801 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. (168 aa)
EAQ12657.1NADH-ubiquinone oxidoreductase; COG0702 Predicted nucleoside-diphosphate-sugar epimerases. (322 aa)
EAQ12504.1COG2857 Cytochrome c1. (265 aa)
EAQ12503.1COG1290 Cytochrome b subunit of the bc complex. (126 aa)
EAQ13948.1COG3256 Nitric oxide reductase large subunit. (448 aa)
EAQ13947.1Nitric oxide reductase subunit C, cytochrome c; COG2010 Cytochrome c, mono- and diheme variants. (127 aa)
EAQ13937.1COG2010 Cytochrome c, mono- and diheme variants. (158 aa)
EAQ13934.1COG2010 Cytochrome c, mono- and diheme variants. (145 aa)
EAQ13400.1COG3278 Cbb3-type cytochrome oxidase, subunit 1; Belongs to the heme-copper respiratory oxidase family. (532 aa)
EAQ13399.1COG2993 Cbb3-type cytochrome oxidase, cytochrome c subunit. (250 aa)
EAQ13397.1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (287 aa)
EAQ13305.1Hypothetical protein. (40 aa)
EAQ13302.1COG2010 Cytochrome c, mono- and diheme variants. (148 aa)
EAQ13255.1Hypothetical protein; COG2804 Type II secretory pathway, ATPase PulE/Tfp pilus assembly pathway, ATPase PilB. (169 aa)
EAQ12203.1NAD dependent formate dehydrogenase, beta subunit (51 kDa); COG1894 NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit. (499 aa)
EAQ12202.1ATP synthase subunit E; COG1905 NADH:ubiquinone oxidoreductase 24 kD subunit. (160 aa)
EAQ12176.1COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family. (557 aa)
EAQ11976.1COG3761 NADH:ubiquinone oxidoreductase 17.2 kD subunit. (124 aa)
EAQ12741.1Cytochrome 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). (282 aa)
EAQ10741.1Cytochrome c550, putative; COG2010 Cytochrome c, mono- and diheme variants. (228 aa)
EAQ11434.1COG3474 Cytochrome c2. (233 aa)
EAQ11433.1COG2010 Cytochrome c, mono- and diheme variants. (354 aa)
nuoBNADH dehydrogenase beta 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. (174 aa)
EAQ12095.1NADH-quinone oxidoreductase, 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. (433 aa)
EAQ12099.1NADH dehydrogenase I, G 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. Belongs to the complex I 75 kDa subunit family. (674 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. (164 aa)
nuoKNADH 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. (121 aa)
Your Current Organism:
Maritimibacter alkaliphilus
NCBI taxonomy Id: 314271
Other names: M. alkaliphilus HTCC2654, Maritimibacter alkaliphilus HTCC2654, Maritimibacter alkaliphilus str. HTCC2654, Maritimibacter alkaliphilus strain HTCC2654, Rhodobacterales bacterium HTCC2654
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