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Noc_0107 Noc_0107 Noc_0164 Noc_0164 Noc_0297 Noc_0297 Noc_0298 Noc_0298 Noc_0299 Noc_0299 Noc_0390 Noc_0390 Noc_0396 Noc_0396 Noc_0462 Noc_0462 Noc_0463 Noc_0463 Noc_0464 Noc_0464 Noc_0465 Noc_0465 Noc_0466 Noc_0466 Noc_0467 Noc_0467 Noc_0470 Noc_0470 Noc_0471 Noc_0471 Noc_0472 Noc_0472 Noc_0474 Noc_0474 Noc_0475 Noc_0475 Noc_0476 Noc_0476 nuoK nuoK Noc_0478 Noc_0478 Noc_0479 Noc_0479 Noc_0480 Noc_0480 nuoN nuoN Noc_0539 Noc_0539 Noc_0540 Noc_0540 Noc_0551 Noc_0551 Noc_0552 Noc_0552 Noc_0751 Noc_0751 Noc_1025 Noc_1025 nuoN1 nuoN1 Noc_1116 Noc_1116 Noc_1117 Noc_1117 nuoK-2 nuoK-2 Noc_1119 Noc_1119 nuoI1 nuoI1 nuoH1 nuoH1 Noc_1122 Noc_1122 Noc_1123 Noc_1123 Noc_1124 Noc_1124 nuoC nuoC nuoB1 nuoB1 nuoA nuoA Noc_1237 Noc_1237 Noc_1238 Noc_1238 Noc_1239 Noc_1239 Noc_1240 Noc_1240 Noc_1241 Noc_1241 Noc_1242 Noc_1242 Noc_1243 Noc_1243 Noc_1244 Noc_1244 Noc_1245 Noc_1245 Noc_1246 Noc_1246 Noc_1247 Noc_1247 Noc_1248 Noc_1248 Noc_1249 Noc_1249 Noc_1250 Noc_1250 Noc_1251 Noc_1251 Noc_1252 Noc_1252 Noc_1279 Noc_1279 Noc_1280 Noc_1280 Noc_1281 Noc_1281 Noc_1282 Noc_1282 Noc_1283 Noc_1283 Noc_1284 Noc_1284 Noc_1285 Noc_1285 Noc_1286 Noc_1286 Noc_1287 Noc_1287 Noc_1288 Noc_1288 Noc_1610 Noc_1610 Noc_1653 Noc_1653 Noc_1766 Noc_1766 Noc_1767 Noc_1767 Noc_1795 Noc_1795 Noc_1796 Noc_1796 Noc_1797 Noc_1797 Noc_1798 Noc_1798 Noc_1799 Noc_1799 Noc_1800 Noc_1800 Noc_1898 Noc_1898 Noc_1908 Noc_1908 Noc_1929 Noc_1929 Noc_1932 Noc_1932 Noc_1933 Noc_1933 Noc_2000 Noc_2000 nuoN2 nuoN2 Noc_2553 Noc_2553 Noc_2554 Noc_2554 nuoK-3 nuoK-3 Noc_2556 Noc_2556 nuoI2 nuoI2 nuoH2 nuoH2 Noc_2559 Noc_2559 Noc_2560 Noc_2560 Noc_2561 Noc_2561 nuoD nuoD nuoC-2 nuoC-2 nuoB2 nuoB2 nuoA-2 nuoA-2 Noc_2609 Noc_2609 Noc_2610 Noc_2610 Noc_2700 Noc_2700 Noc_2701 Noc_2701 Noc_2702 Noc_2702 Noc_2769 Noc_2769 Noc_2898 Noc_2898 Noc_2899 Noc_2899 Noc_2900 Noc_2900 Noc_2901 Noc_2901 Noc_2968 Noc_2968 Noc_2969 Noc_2969 Noc_2970 Noc_2970 Noc_2971 Noc_2971 cyoE cyoE Noc_3040 Noc_3040 Noc_3041 Noc_3041 Noc_3042 Noc_3042 Noc_3043 Noc_3043 Noc_3044 Noc_3044 Noc_3045 Noc_3045 Noc_3046 Noc_3046 Noc_3047 Noc_3047 Noc_3048 Noc_3048 Noc_3049 Noc_3049 Noc_3050 Noc_3050
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:
Noc_0107NAD-dependent epimerase/dehydratase. (308 aa)
Noc_0164High-affinity Fe2+/Pb2+ permease. (653 aa)
Noc_0297Cytochrome c1. (240 aa)
Noc_0298Cytochrome b/b6-like protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (408 aa)
Noc_0299Ubiquinol-cytochrome c reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (201 aa)
Noc_0390NAD-dependent epimerase/dehydratase. (320 aa)
Noc_0396Conserved hypothetical protein. (134 aa)
Noc_0462Protein of unknown function DUF202. (127 aa)
Noc_0463Protein of unknown function DUF1362. (125 aa)
Noc_0464Conserved hypothetical protein. (984 aa)
Noc_0465Putative membrane protein. (323 aa)
Noc_0466Conserved hypothetical protein. (213 aa)
Noc_0467Glucose-methanol-choline oxidoreductase. (548 aa)
Noc_0470Mandelate racemase/muconate lactonizing enzyme. (367 aa)
Noc_0471Pyruvate oxidase; Belongs to the TPP enzyme family. (601 aa)
Noc_0472Short-chain dehydrogenase/reductase SDR; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (328 aa)
Noc_0474NADH dehydrogenase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (105 aa)
Noc_0475NADH dehydrogenase subunit H. (310 aa)
Noc_0476NADH 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. (265 aa)
nuoKNADH dehydrogenase subunit K; 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. (104 aa)
Noc_0478NADH dehydrogenase subunit L. (548 aa)
Noc_0479Hypothetical protein. (111 aa)
Noc_0480NADH dehydrogenase subunit M. (491 aa)
nuoNNADH dehydrogenase subunit N; 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 2 family. (470 aa)
Noc_0539ABC transporter, ATPase subunit. (251 aa)
Noc_0540ABC transporter, fused inner membrane component and substrate-binding domain. (501 aa)
Noc_0551DSBA oxidoreductase. (220 aa)
Noc_0552Cytochrome c, class I. (209 aa)
Noc_0751Cytochrome c, class I. (112 aa)
Noc_1025Patatin. (453 aa)
nuoN1NADH dehydrogenase subunit N; 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 2 family. (481 aa)
Noc_1116NADH dehydrogenase subunit M. (493 aa)
Noc_1117NADH dehydrogenase subunit L. (657 aa)
nuoK-2NADH dehydrogenase subunit K; 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. (103 aa)
Noc_1119NADH 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. (167 aa)
nuoI1NADH 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. (180 aa)
nuoH1NADH dehydrogenase subunit H; 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. This subunit may bind ubiquinone. (319 aa)
Noc_1122NADH dehydrogenase subunit G; 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. (909 aa)
Noc_1123NADH dehydrogenase subunit F; 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. (429 aa)
Noc_1124NADH dehydrogenase subunit E. (154 aa)
nuoCNADH dehydrogenase subunit D / NADH dehydrogenase subunit C; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (593 aa)
nuoB1NADH dehydrogenase subunit B; 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. (212 aa)
nuoANADH dehydrogenase subunit A; 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 3 family. (129 aa)
Noc_1237Quinol:cytochrome c oxidoreductase pentaheme cytochrome subunit. (214 aa)
Noc_1238Quinol:cytochrome c oxidoreductase iron-sulfur protein precursor. (993 aa)
Noc_1239Quinol:cytochrome c oxidoreductase quinone-binding subunit 1. (454 aa)
Noc_1240Quinol:cytochrome c oxidoreductase membrane protein. (180 aa)
Noc_1241Quinol:cytochrome c oxidoreductase monoheme cytochrome subunit. (213 aa)
Noc_1242Quinol:cytochrome c oxidoreductase quinone-binding subunit 2. (392 aa)
Noc_1243Hypothetical protein. (139 aa)
Noc_1244Cytochrome 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). (211 aa)
Noc_1245Cytochrome 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. (535 aa)
Noc_1246Cytochrome/quinol oxidase subunit 3. (214 aa)
Noc_1247Caa(3)-type oxidase, subunit IV. (230 aa)
Noc_1248NADH dehydrogenase subunit M. (512 aa)
Noc_1249NADH dehydrogenase subunit M. (513 aa)
Noc_1250NADH dehydrogenase (quinone). (513 aa)
Noc_1251Conserved hypothetical protein; Belongs to the UPF0753 family. (1125 aa)
Noc_1252NADH dehydrogenase subunit M. (485 aa)
Noc_1279NADH/Ubiquinone/plastoquinone (complex I). (565 aa)
Noc_1280NADH dehydrogenase (quinone). (499 aa)
Noc_1281Multisubunit sodium/proton antiporter, MrpD subunit; TC 2.A.63.1. (493 aa)
Noc_1282Multisubunit sodium/proton antiporter, MrpC subunit; TC 2.A.63.1. (105 aa)
Noc_1283Conserved hypothetical protein. (236 aa)
Noc_1284Hypothetical protein. (96 aa)
Noc_1285Multisubunit sodium/proton antiporter, MrpG subunit; TC 2.A.63.1. (104 aa)
Noc_1286Multisubunit sodium/proton antiporter, MrpF subunit; TC 2.A.63.1. (95 aa)
Noc_1287Cation antiporter. (165 aa)
Noc_1288Universal stress protein UspA. (310 aa)
Noc_1610Hypothetical protein. (479 aa)
Noc_1653Hypothetical protein. (170 aa)
Noc_1766Cytochrome c oxidase; Belongs to the heme-copper respiratory oxidase family. (853 aa)
Noc_1767Cytochrome c oxidase, subunit II. (352 aa)
Noc_1795Hypothetical protein. (680 aa)
Noc_1796Glucose-methanol-choline oxidoreductase. (703 aa)
Noc_1797Conserved hypothetical protein. (483 aa)
Noc_1798Conserved hypothetical protein. (506 aa)
Noc_1799NADH-flavin oxidoreductase/NADH oxidase. (441 aa)
Noc_1800Hypothetical protein. (723 aa)
Noc_1898Conserved hypothetical protein. (575 aa)
Noc_1908Conserved hypothetical protein, RDD. (154 aa)
Noc_19294Fe-4S ferredoxin, iron-sulfur binding protein. (84 aa)
Noc_1932Peptidase M16-like protein. (434 aa)
Noc_1933Peptidase M16-like protein; Belongs to the peptidase M16 family. (459 aa)
Noc_2000Cytochrome c, class I. (192 aa)
nuoN2NADH dehydrogenase subunit N; 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 2 family. (478 aa)
Noc_2553NADH dehydrogenase subunit M. (504 aa)
Noc_2554NADH dehydrogenase subunit L. (650 aa)
nuoK-3NADH dehydrogenase subunit K; 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. (101 aa)
Noc_2556NADH 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. (201 aa)
nuoI2NADH 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. (162 aa)
nuoH2NADH dehydrogenase subunit H; 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. This subunit may bind ubiquinone. (344 aa)
Noc_2559NADH dehydrogenase subunit G; 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. (797 aa)
Noc_2560NADH dehydrogenase subunit F; 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. (427 aa)
Noc_2561NADH dehydrogenase subunit E. (175 aa)
nuoDNADH dehydrogenase subunit D; 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 49 kDa subunit family. (417 aa)
nuoC-2NADH dehydrogenase subunit C; 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 30 kDa subunit family. (231 aa)
nuoB2NADH dehydrogenase subunit B; 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 (By similarity). (158 aa)
nuoA-2NADH dehydrogenase subunit A; 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 3 family. (118 aa)
Noc_2609Cold-shock DNA-binding protein family. (69 aa)
Noc_2610RNA-binding protein, RNP-1. (91 aa)
Noc_2700Conserved hypothetical protein. (169 aa)
Noc_2701Conserved hypothetical protein. (169 aa)
Noc_2702Conserved hypothetical protein. (281 aa)
Noc_2769RNA-binding protein, RNP-1. (119 aa)
Noc_2898Hypothetical protein. (81 aa)
Noc_2899Conserved hypothetical protein. (439 aa)
Noc_2900Electron transport protein SCO1/SenC. (196 aa)
Noc_2901Conserved hypothetical protein. (209 aa)
Noc_2968Putative transmembrane protein. (206 aa)
Noc_2969Electron transport protein SCO1/SenC. (208 aa)
Noc_2970Cytochrome c oxidase, subunit I. (499 aa)
Noc_2971Cytochrome c oxidase, subunit II. (176 aa)
cyoEProtoheme 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. (299 aa)
Noc_3040Cytochrome oxidase assembly. (342 aa)
Noc_3041Conserved hypothetical protein. (204 aa)
Noc_3042Conserved hypothetical protein. (243 aa)
Noc_3043Hypothetical protein. (97 aa)
Noc_3044Cytochrome c oxidase, subunit III. (288 aa)
Noc_3045Cytochrome c oxidase assembly protein CtaG/Cox11. (210 aa)
Noc_3046Cytochrome 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. (532 aa)
Noc_3047Cytochrome 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). (281 aa)
Noc_3048Conserved hypothetical protein. (158 aa)
Noc_3049Cytochrome c, class I. (113 aa)
Noc_3050Cytochrome c, class I. (106 aa)
Your Current Organism:
Nitrosococcus oceani
NCBI taxonomy Id: 323261
Other names: N. oceani ATCC 19707, Nitrosococcus oceani ATCC 19707, Nitrosococcus oceani C-107, Nitrosococcus oceani NCIMB 11848, Nitrosococcus oceani str. ATCC 19707, Nitrosococcus oceani strain ATCC 19707
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