STRINGSTRING
AFW93099.1 AFW93099.1 coxC coxC coxA coxA coxB coxB patB patB aspA aspA AFW93525.1 AFW93525.1 AFW93546.1 AFW93546.1 AFW93619.1 AFW93619.1 ndhL ndhL AFW93687.1 AFW93687.1 sucC sucC sucD sucD nuoM nuoM AFW94137.1 AFW94137.1 AFW94252.1 AFW94252.1 ndhD ndhD ndhF ndhF AFW94265.1 AFW94265.1 AFW94323.1 AFW94323.1 nuoM-2 nuoM-2 hoxU hoxU hoxF hoxF hoxE hoxE nifJ nifJ ndhE ndhE ndhG ndhG ndhI ndhI ndhA-2 ndhA-2 AFW95270.1 AFW95270.1 ndhD4 ndhD4 ndhF3 ndhF3 AFW95300.1 AFW95300.1 AFW95454.1 AFW95454.1 AFW95455.1 AFW95455.1 AFW95456.1 AFW95456.1 AFW95662.1 AFW95662.1 sdhA sdhA coxC-2 coxC-2 coxA-2 coxA-2 coxB-2 coxB-2 AFW95868.1 AFW95868.1 ctaB ctaB ndhF-2 ndhF-2 AFW96265.1 AFW96265.1 dhsB dhsB ndhB ndhB ndhC ndhC ndhK ndhK ndhJ ndhJ nifJ-2 nifJ-2 hdrB hdrB acnB acnB ndhD2 ndhD2 ndhH ndhH coxC-3 coxC-3 coxA-3 coxA-3 coxB-3 coxB-3
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.
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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:
AFW93099.1Pyridine nucleotide-disulfide oxidoreductase. (580 aa)
coxCCytochrome c oxidase subunit III protein. (198 aa)
coxACytochrome c oxidase subunit I protein; 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. (557 aa)
coxBCytochrome c oxidase subunit II protein; 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). (311 aa)
patB4Fe-4S ferredoxin iron-sulfur binding domain-containing protein. (528 aa)
aspAAspartate ammonia-lyase. (469 aa)
AFW93525.1Hypothetical protein. (629 aa)
AFW93546.1Isocitrate dehydrogenase. (473 aa)
AFW93619.1NmrA family protein. (333 aa)
ndhLNADH dehydrogenase subunit NdhL. (71 aa)
AFW93687.1Thioredoxin (TRX)-like [2Fe-2S] ferredoxin-domain containing protein. (181 aa)
sucCsuccinyl-CoA synthetase beta subunit. (412 aa)
sucDsuccinyl-CoA synthetase alpha subunit. (300 aa)
nuoMProton-translocating NADH-quinone oxidoreductase chain M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 4 family. (534 aa)
AFW94137.1Iron-sulfur cluster-binding protein. (134 aa)
AFW94252.1CO2 hydration protein. (440 aa)
ndhDProton-translocating NADH-quinone oxidoreductase chain M. (497 aa)
ndhFNAD(P)H dehydrogenase subunit NdhF3. (619 aa)
AFW94265.1Fasciclin-like domain-containing protein. (133 aa)
AFW94323.1Alpha/beta hydrolase fold-containing protein. (300 aa)
nuoM-2NADH dehydrogenase subunit M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 4 family. (525 aa)
hoxUHydrogenase subunit HoxU. (238 aa)
hoxFHydrogenase subunit HoxF. (534 aa)
hoxEHydrogenase subunit HoxE. (170 aa)
nifJPyruvate-flavodoxin oxidoreductase NifJ; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin. (1208 aa)
ndhENADH dehydrogenase subunit 4L; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (101 aa)
ndhGNADH dehydrogenase subunit 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. Belongs to the complex I subunit 6 family. (203 aa)
ndhINADH dehydrogenase subunit I; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family. (191 aa)
ndhA-2NADH dehydrogenase subunit 1; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (372 aa)
AFW95270.1Hypothetical protein. (206 aa)
ndhD4NAD(P)H-quinone oxidoreductase subunit D4. (498 aa)
ndhF3NAD(P)H-quinone oxidoreductase subunit F. (618 aa)
AFW95300.14Fe-4S ferredoxin type iron-sulfur binding protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (75 aa)
AFW95454.1Transcriptional regulator, TetR family. (204 aa)
AFW95455.1Peptidase M16; Belongs to the peptidase M16 family. (525 aa)
AFW95456.1Peptidase M16. (501 aa)
AFW95662.1Aldehyde dehydrogenase. (455 aa)
sdhASuccinate dehydrogenase flavoprotein subunit. (575 aa)
coxC-2Cytochrome c oxidase subunit III. (204 aa)
coxA-2Cytochrome 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. (557 aa)
coxB-2Cytochrome 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). (321 aa)
AFW95868.1Cytochrome oxidase assembly protein. (308 aa)
ctaBProtoheme 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. (312 aa)
ndhF-2NADH-plastoquinone oxidoreductase subunit F. (692 aa)
AFW96265.1Peptidase M16 family protein; Belongs to the peptidase M16 family. (425 aa)
dhsBSuccinate dehydrogenase/fumarate reductase iron-sulfur protein. (378 aa)
ndhBProton-translocating NADH-quinone oxidoreductase chain N; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (520 aa)
ndhCNADH dehydrogenase subunit A; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (120 aa)
ndhKNADH dehydrogenase subunit B; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. (245 aa)
ndhJNADH dehydrogenase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (175 aa)
nifJ-2Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin. (1195 aa)
hdrBHeterodisulfide reductase subunit B. (301 aa)
acnBAconitate hydratase 2; Belongs to the aconitase/IPM isomerase family. (876 aa)
ndhD2Proton-translocating NADH-quinone oxidoreductase chain M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 4 family. (562 aa)
ndhHNAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (394 aa)
coxC-3Cytochrome c oxidase, subunit III. (200 aa)
coxA-3Cytochrome 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. (550 aa)
coxB-3Cytochrome 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). (308 aa)
Your Current Organism:
Anabaena sp. 90
NCBI taxonomy Id: 46234
Other names: A. sp. 90, Anabaena circinalis 90, Anabaena sp. strain 90
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