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Tery_0033 Tery_0033 Tery_0276 Tery_0276 Tery_0277 Tery_0277 Tery_0278 Tery_0278 Tery_0349 Tery_0349 Tery_0579 Tery_0579 ndhD1 ndhD1 Tery_0660 Tery_0660 Tery_0914 Tery_0914 Tery_0915 Tery_0915 Tery_0916 Tery_0916 Tery_0966 Tery_0966 Tery_1003 Tery_1003 Tery_1567 Tery_1567 ndhE ndhE Tery_1577 Tery_1577 ndhI ndhI ndhA ndhA Tery_1777 Tery_1777 Tery_1778 Tery_1778 Tery_1779 Tery_1779 Tery_1780 Tery_1780 ctaB ctaB petC petC Tery_1885 Tery_1885 Tery_1949 Tery_1949 Tery_2109 Tery_2109 ndhB ndhB Tery_2773 Tery_2773 Tery_2774 Tery_2774 Tery_3162 Tery_3162 ndhD2 ndhD2 Tery_3410 Tery_3410 ndhJ ndhJ ndhK ndhK ndhC ndhC Tery_3563 Tery_3563 Tery_3658 Tery_3658 Tery_3821 Tery_3821 Tery_3853 Tery_3853 Tery_3956 Tery_3956 Tery_4342 Tery_4342 Tery_4504 Tery_4504 Tery_4539 Tery_4539 Tery_4583 Tery_4583 ndhH ndhH
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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:
Tery_0033PFAM: protein of unknown function DUF477; KEGG: ava:Ava_0806 protein of unknown function DUF477. (242 aa)
Tery_0276PFAM: cytochrome c oxidase, subunit III; KEGG: ava:Ava_4300 cytochrome c oxidase subunit III. (204 aa)
Tery_0277Cytochrome-c oxidase; 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. (562 aa)
Tery_0278Cytochrome 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). (302 aa)
Tery_0349KEGG: ava:Ava_4474 NADH dehydrogenase subunit M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (506 aa)
Tery_05794Fe-4S ferredoxin, iron-sulfur binding; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (75 aa)
ndhD1Proton-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. (527 aa)
Tery_0660Proton-translocating NADH-quinone oxidoreductase, chain L; KEGG: syn:slr0844 NADH dehydrogenase I subunit 5, involved in photosystem-1 cyclic electron flow; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5/L-like NADH/Ubiquinone/plastoquinone (complex I). (687 aa)
Tery_0914TIGRFAM: ferredoxin [2Fe-2S]; PFAM: ferredoxin; KEGG: gvi:gsr3623 ferredoxin. (96 aa)
Tery_0915TIGRFAM: ferredoxin [2Fe-2S]; PFAM: ferredoxin; KEGG: cyb:CYB_1598 ferredoxin, 2Fe-2S. (100 aa)
Tery_0916TIGRFAM: ferredoxin [2Fe-2S]; PFAM: ferredoxin; KEGG: gvi:gsr3623 ferredoxin. (98 aa)
Tery_0966PFAM: peptidase M16-like; KEGG: ana:alr2744 processing protease. (413 aa)
Tery_1003NmrA-like; PFAM: NAD-dependent epimerase/dehydratase 3-beta hydroxysteroid dehydrogenase/isomerase NmrA-like Male sterility-like; KEGG: ana:alr2751 hypothetical protein. (221 aa)
Tery_1567Ferredoxin thioredoxin reductase, beta chain; Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin. (121 aa)
ndhENADH-ubiquinone oxidoreductase, chain 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. (108 aa)
Tery_1577NADH-ubiquinone/plastoquinone oxidoreductase, chain 6; 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. (207 aa)
ndhINADH-plastoquinone oxidoreductase, I 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; Belongs to the complex I 23 kDa subunit family. (209 aa)
ndhARespiratory-chain NADH 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)
Tery_1777PFAM: cytochrome c oxidase, subunit III; KEGG: tel:tll2009 cytochrome c oxidase subunit III. (211 aa)
Tery_1778Cytochrome-c oxidase; 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. (590 aa)
Tery_1779Cytochrome 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). (339 aa)
Tery_1780PFAM: cytochrome oxidase assembly; KEGG: ava:Ava_0527 cytochrome oxidase assembly. (304 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. (328 aa)
petCRieske (2Fe-2S) region; 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. Belongs to the Rieske iron-sulfur protein family. (179 aa)
Tery_1885PFAM: 4Fe-4S ferredoxin, iron-sulfur binding; KEGG: ava:Ava_0445 4Fe-4S ferredoxin, iron-sulfur binding. (99 aa)
Tery_1949PFAM: ferredoxin thioredoxin reductase, alpha chain; KEGG: ava:Ava_0401 ferredoxin thioredoxin reductase, alpha chain. (73 aa)
Tery_2109PFAM: AMP-dependent synthetase and ligase Thioesterase phosphopantetheine-binding; KEGG: ava:Ava_4108 beta-ketoacyl synthase. (991 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. (526 aa)
Tery_2773PFAM: peptidase M16-like; KEGG: ana:all1940 protease; Belongs to the peptidase M16 family. (550 aa)
Tery_2774PFAM: peptidase M16-like; KEGG: ana:all1939 processing proteinase. (494 aa)
Tery_3162NmrA-like; PFAM: NAD-dependent epimerase/dehydratase 3-beta hydroxysteroid dehydrogenase/isomerase NmrA-like; KEGG: ana:all4752 hypothetical protein. (325 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. (561 aa)
Tery_3410Hypothetical protein. (122 aa)
ndhJNADH dehydrogenase (ubiquinone), 30 kDa 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. (167 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. (240 aa)
ndhCNADH-ubiquinone/plastoquinone oxidoreductase, chain 3; 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. (135 aa)
Tery_3563NmrA-like; PFAM: NAD-dependent epimerase/dehydratase 3-beta hydroxysteroid dehydrogenase/isomerase NmrA-like; KEGG: ava:Ava_2558 3-beta hydroxysteroid dehydrogenase/isomerase. (291 aa)
Tery_3658PFAM: oxidoreductase FAD/NAD(P)-binding CpcD phycobilisome linker-like; KEGG: ava:Ava_0782 oxidoreductase FAD/NAD(P)-binding. (405 aa)
Tery_3821PFAM: beta-ketoacyl synthase acyl transferase region short-chain dehydrogenase/reductase SDR phosphopantetheine-binding; KEGG: ava:Ava_3986 short-chain dehydrogenase/reductase SDR. (1909 aa)
Tery_3853KEGG: ana:alr0869 NADH dehydrogenase subunit 5; TIGRFAM: NAD(P)H dehydrogenase, subunit NdhF3 family; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (614 aa)
Tery_3956PFAM: ferredoxin; KEGG: syn:ssr1041 NAD-reducing hydrogenase gamma subunit homolog. (77 aa)
Tery_4342PFAM: peptidase M16-like; KEGG: ana:alr5125 processing protease; Belongs to the peptidase M16 family. (431 aa)
Tery_4504PFAM: ferredoxin; KEGG: tel:tll1529 probable ferredoxin. (102 aa)
Tery_4539TIGRFAM: ferredoxin [2Fe-2S]; PFAM: ferredoxin; KEGG: ava:Ava_0568 ferredoxin (2Fe-2S). (111 aa)
Tery_4583Male sterility-like; PFAM: NAD-dependent epimerase/dehydratase NmrA-like Male sterility-like; KEGG: ath:At4g31530 expressed protein. (282 aa)
ndhHNADH dehydrogenase (ubiquinone); 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)
Your Current Organism:
Trichodesmium erythraeum
NCBI taxonomy Id: 203124
Other names: T. erythraeum IMS101, Trichodesmium erythraeum IMS101, Trichodesmium erythraeum str. IMS101, Trichodesmium erythraeum strain IMS101, Trichodesmium sp. IMS101
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