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EKF01164.1 EKF01164.1 EKE99458.1 EKE99458.1 EKE99623.1 EKE99623.1 ndhI ndhI ndhE ndhE EKF00081.1 EKF00081.1 EKF00373.1 EKF00373.1 EKF00357.1 EKF00357.1 ndhD-3 ndhD-3 EKF00710.1 EKF00710.1 EKF01467.1 EKF01467.1 EKF02096.1 EKF02096.1 EKF02048.1 EKF02048.1 EKF02047.1 EKF02047.1 EKE97154.1 EKE97154.1 EKE97464.1 EKE97464.1 EKE97463.1 EKE97463.1 EKE97833.1 EKE97833.1 EKE97831.1 EKE97831.1 EKE97830.1 EKE97830.1 EKE98780.1 EKE98780.1 EKE98779.1 EKE98779.1 EKE98669.1 EKE98669.1 EKE98668.1 EKE98668.1 ndhK ndhK EKE98935.1 EKE98935.1 ndhD-2 ndhD-2 ndhD ndhD EKF04500.1 EKF04500.1 EKF04499.1 EKF04499.1 EKF04498.1 EKF04498.1 EKF05194.1 EKF05194.1 EKF05859.1 EKF05859.1 EKF05858.1 EKF05858.1 EKF05806.1 EKF05806.1 EKF05805.1 EKF05805.1 EKF05885.1 EKF05885.1 petB petB
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:
EKF01164.1Hypothetical protein; KEGG: syg:sync_0549 4.1e-20 petB; cytochrome b6 K02635; Psort location: CytoplasmicMembrane, score: 10.00. (188 aa)
EKE99458.1Putative glutathione gamma-glutamylcysteinyltransferase; KEGG: cbd:CBUD_1504 2.8e-44 phytochelatin synthase. (246 aa)
EKE99623.1KEGG: npu:Npun_R1526 0. molybdopterin oxidoreductase NarB; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. (747 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. (194 aa)
ndhENADH dehydrogenase subunit 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. (101 aa)
EKF00081.14Fe-4S binding domain protein; KEGG: mbu:Mbur_0285 7.3e-10 formylmethanofuran dehydrogenase, subunit F K00205; Psort location: Cytoplasmic, score: 8.96. (151 aa)
EKF00373.1KEGG: npu:Npun_F4648 6.8e-66 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase K00950; Psort location: Cytoplasmic, score: 8.96. (189 aa)
EKF00357.1NAD(P)H-quinone oxidoreductase subunit D4; KEGG: npu:Npun_R4289 6.0e-225 proton-translocating NADH-quinone oxidoreductase, chain M K05575; Psort location: CytoplasmicMembrane, score: 10.00. (499 aa)
ndhD-3Proton-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. (537 aa)
EKF00710.1Hypothetical protein; KEGG: ava:Ava_2796 1.5e-61 NAD(P)H-quinone oxidoreductase subunit 4 K05575. (146 aa)
EKF01467.1Putative thioredoxin; KEGG: pth:PTH_2011 6.8e-07 nuoF; NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit; K00335 NADH dehydrogenase I subunit F; Psort location: Cytoplasmic, score: 8.96. (178 aa)
EKF02096.1KEGG: ana:alr0762 1.0e-117 hoxU; bidirectional hydrogenase complex protein HoxU; K05588 diaphorase subunit of the bidirectional hydrogenase; Psort location: Cytoplasmic, score: 9.97. (238 aa)
EKF02048.1Cytochrome 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. (552 aa)
EKF02047.1Cytochrome c oxidase subunit; 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). (281 aa)
EKE97154.1KEGG: npu:Npun_F5945 1.9e-157 succinate dehydrogenase and fumarate reductase iron-sulfur protein K00240; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (335 aa)
EKE97464.1H(+)-transporting two-sector protein; KEGG: ava:Ava_4653 1.4e-65 bidirectional hydrogenase complex protein HoxE K05586; Psort location: Cytoplasmic, score: 9.26. (181 aa)
EKE97463.1Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. (548 aa)
EKE97833.1KEGG: ava:Ava_3575 4.7e-106 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (222 aa)
EKE97831.1Cytochrome 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. (561 aa)
EKE97830.1Cytochrome 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). (306 aa)
EKE98780.1Cytochrome 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. (578 aa)
EKE98779.1Cytochrome c oxidase subunit; 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). (365 aa)
EKE98669.1Cytochrome 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). (325 aa)
EKE98668.1Cytochrome 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. (560 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)
EKE98935.1Peptidase, U32 family; KEGG: npu:Npun_R3500 0. peptidase U32; K08303 putative protease; Psort location: Extracellular, score: 9.52. (860 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. (562 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. (524 aa)
EKF04500.1KEGG: ava:Ava_B0177 7.4e-108 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (239 aa)
EKF04499.1Cytochrome 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. (558 aa)
EKF04498.1Cytochrome c oxidase subunit; 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). (298 aa)
EKF05194.1Hypothetical protein; KEGG: det:DET0729 5.0e-07 [Fe] hydrogenase, HymB subunit, putative; K00335 NADH dehydrogenase I subunit F. (216 aa)
EKF05859.1KEGG: npu:Npun_R3535 1.7e-92 cytochrome c oxidase, subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (200 aa)
EKF05858.1KEGG: ana:alr2732 6.5e-235 coxA; cytochrome c oxidase subunit I; K02274 cytochrome c oxidase subunit I; Psort location: CytoplasmicMembrane, score: 10.00; Belongs to the heme-copper respiratory oxidase family. (457 aa)
EKF05806.1KEGG: ana:alr2732 4.7e-42 coxA; cytochrome c oxidase subunit I; K02274 cytochrome c oxidase subunit I; Psort location: CytoplasmicMembrane, score: 9.82. (105 aa)
EKF05805.1Cytochrome c oxidase; 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)
EKF05885.1NAD(P)H-quinone oxidoreductase subunit M; KEGG: npu:Npun_F3688 1.8e-230 proton-translocating NADH-quinone oxidoreductase, chain M K05575; Psort location: CytoplasmicMembrane, score: 10.00. (499 aa)
petBCytochrome b6; 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. (215 aa)
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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