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AFZ48881.1 AFZ48881.1 AFZ48883.1 AFZ48883.1 AFZ48940.1 AFZ48940.1 AFZ48941.1 AFZ48941.1 AFZ48942.1 AFZ48942.1 AFZ48943.1 AFZ48943.1 ctaB ctaB AFZ49112.1 AFZ49112.1 AFZ49113.1 AFZ49113.1 AFZ49779.1 AFZ49779.1 AFZ50216.1 AFZ50216.1 ndhH ndhH AFZ50346.1 AFZ50346.1 AFZ50347.1 AFZ50347.1 AFZ50348.1 AFZ50348.1 AFZ50421.1 AFZ50421.1 AFZ50422.1 AFZ50422.1 AFZ50470.1 AFZ50470.1 AFZ50521.1 AFZ50521.1 ndhM ndhM AFZ50808.1 AFZ50808.1 petB petB ndhA ndhA ndhI ndhI AFZ51110.1 AFZ51110.1 ndhE ndhE ndhD ndhD AFZ51360.1 AFZ51360.1 ndhO ndhO ndhL ndhL ndhB ndhB AFZ51664.1 AFZ51664.1 AFZ51782.1 AFZ51782.1 ndhC ndhC ndhK ndhK ndhJ ndhJ ndhD-2 ndhD-2 AFZ51990.1 AFZ51990.1 ndhN ndhN
Nodes:
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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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
AFZ48881.1Putative hydrolase or acyltransferase of alpha/beta superfamily. (204 aa)
AFZ48883.1PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit. (191 aa)
AFZ48940.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. (204 aa)
AFZ48941.1Cytochrome 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. (555 aa)
AFZ48942.1Heme/copper-type cytochrome/quinol oxidases, subunit 2; 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). (355 aa)
AFZ48943.1PFAM: Cytochrome oxidase assembly protein. (307 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. (316 aa)
AFZ49112.1Putative Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16); Belongs to the peptidase M16 family. (505 aa)
AFZ49113.1Putative Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16). (482 aa)
AFZ49779.1Putative Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16); Belongs to the peptidase M16 family. (425 aa)
AFZ50216.1Putative nucleoside-diphosphate sugar epimerase; PFAM: NmrA-like family. (253 aa)
ndhHNADH dehydrogenase I, D subunit; 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)
AFZ50346.1PFAM: CO2 hydration protein (ChpXY); TIGRFAM: CO2 hydration protein. (428 aa)
AFZ50347.1PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (521 aa)
AFZ50348.1NAD(P)H dehydrogenase, subunit NdhF3 family; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TIGRFAM: NAD(P)H dehydrogenase, subunit NdhF3 family. (609 aa)
AFZ50421.1PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (500 aa)
AFZ50422.1NAD(P)H dehydrogenase, subunit NdhF3 family; PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; NADH-Ubiquinone/plastoquinone (complex I), various chains; TIGRFAM: NAD(P)H dehydrogenase, subunit NdhF3 family. (619 aa)
AFZ50470.1Secreted/surface protein with fasciclin-like repeats; PFAM: Fasciclin domain. (133 aa)
AFZ50521.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (75 aa)
ndhMCyanobacterial and plastid NDH-1 subunit M; 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. (119 aa)
AFZ50808.1Putative Zn-dependent peptidase; PFAM: Peptidase M16 inactive domain; Insulinase (Peptidase family M16). (417 aa)
petBCytochrome b subunit of the bc complex; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. (222 aa)
ndhANADH:ubiquinone oxidoreductase subunit 1 (chain 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. (372 aa)
ndhINADH-plastoquinone oxidoreductase subunit I protein; 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. (210 aa)
AFZ51110.1NADH: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. Belongs to the complex I subunit 6 family. (205 aa)
ndhENADH:ubiquinone oxidoreductase subunit 11 or 4L (chain K); 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. (103 aa)
ndhDProton-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. (547 aa)
AFZ51360.1PFAM: Protein of unknown function (DUF3252). (62 aa)
ndhOCyanobacterial and plant NDH-1 subunit O; 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. (71 aa)
ndhLNADH dehydrogenase transmembrane subunit; 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. (68 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. (527 aa)
AFZ51664.1PFAM: Protein of unknown function (DUF2996). (146 aa)
AFZ51782.1Beta-propeller domain-containing protein, methanol dehydrogenase; PFAM: Domain of unknown function (DUF477). (242 aa)
ndhCNADH:ubiquinone oxidoreductase subunit 3 (chain 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-quinone oxidoreductase, B subunit; 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. (250 aa)
ndhJNADH/F420H2 dehydrogenase, subunit C; 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. (176 aa)
ndhD-2Proton-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. (526 aa)
AFZ51990.1Proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5 C-terminus; NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L. (679 aa)
ndhNNADH-quinone oxidoreductase cyanobacterial subunit 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. (158 aa)
Your Current Organism:
Dactylococcopsis salina
NCBI taxonomy Id: 13035
Other names: D. salina PCC 8305, Dactylococcopsis salina PCC 8305, Dactylococcopsis sp. PCC 8305, Myxobactron salinum PCC 8305
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