STRINGSTRING
ABI64377.1 ABI64377.1 ABI64478.1 ABI64478.1 ABI64480.1 ABI64480.1 ABI64481.1 ABI64481.1 ABI64644.1 ABI64644.1 ABI64645.1 ABI64645.1 ABI64724.1 ABI64724.1 ABI65029.1 ABI65029.1 ABI65030.1 ABI65030.1 ABI65031.1 ABI65031.1 ABI65068.1 ABI65068.1 ABI65126.1 ABI65126.1 ABI65183.1 ABI65183.1 ABI65184.1 ABI65184.1 ABI65186.1 ABI65186.1 ABI65383.1 ABI65383.1 ABI65442.1 ABI65442.1 ABI65443.1 ABI65443.1 ABI65445.1 ABI65445.1 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD ABI65651.1 ABI65651.1 ABI65652.1 ABI65652.1 ABI65653.1 ABI65653.1 ABI65656.1 ABI65656.1 nuoK nuoK ABI65658.1 ABI65658.1 ABI65659.1 ABI65659.1 nuoN nuoN msrQ msrQ ABI65788.1 ABI65788.1 ABI65936.1 ABI65936.1 ABI65955.1 ABI65955.1 ABI66058.1 ABI66058.1 ABI66127.1 ABI66127.1 ABI66189.1 ABI66189.1 ABI66271.1 ABI66271.1 ABI66272.1 ABI66272.1 ABI66290.1 ABI66290.1 ABI66480.1 ABI66480.1 ABI66521.1 ABI66521.1 ABI66525.1 ABI66525.1 ABI66526.1 ABI66526.1 ABI66587.1 ABI66587.1 ABI66655.1 ABI66655.1 ABI66656.1 ABI66656.1 azoR azoR ABI66968.1 ABI66968.1 ABI66969.1 ABI66969.1 ABI66970.1 ABI66970.1 ABI67125.1 ABI67125.1 ABI67127.1 ABI67127.1 ABI67129.1 ABI67129.1
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:
ABI64377.1PFAM: ferredoxin; KEGG: ccr:CC3524 ferredoxin, 2Fe-2S. (106 aa)
ABI64478.1TIGRFAM: pseudoazurin; PFAM: blue (type 1) copper domain protein; KEGG: sme:SMa1243 Azu1 pseudoazurin (blue copper protein). (151 aa)
ABI64480.1PFAM: cytochrome c, class I; KEGG: tbd:Tbd_0146 probable cytochrome c5. (220 aa)
ABI64481.1Ubiquinol-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. (175 aa)
ABI64644.1PFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: rfr:Rfer_2799 pyruvate flavodoxin/ferredoxin oxidoreductase-like. (611 aa)
ABI64645.1PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; KEGG: eba:ebA4589 2-ketoglutarate: NADP oxidoreductase, beta subunit. (350 aa)
ABI64724.1PFAM: cytochrome c, class I; KEGG: eli:ELI_10285 cytochrome c. (236 aa)
ABI65029.1Ubiquinol-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. (207 aa)
ABI65030.1Cytochrome b/b6; 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. (428 aa)
ABI65031.1PFAM: cytochrome c1; KEGG: ccr:CC0474 ubiquinol-cytochrome c reductase cytochrome c1 subunit. (269 aa)
ABI65068.1PFAM: protein of unknown function DUF405; protein of unknown function DUF418; KEGG: nph:NP3452A hypothetical protein. (401 aa)
ABI65126.1PFAM: cytochrome B561; KEGG: rpc:RPC_2322 cytochrome b561. (192 aa)
ABI65183.1Multisubunit sodium/proton antiporter, MrpD subunit; PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: rru:Rru_A1635 NADH dehydrogenase (quinone); TC 2.A.63.1. (507 aa)
ABI65184.1Multisubunit sodium/proton antiporter, MrpD subunit; PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: rru:Rru_A1634 NADH dehydrogenase (quinone); TC 2.A.63.1. (493 aa)
ABI65186.1Multisubunit sodium/proton antiporter, MrpD subunit; PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: rba:RB1427 putative NADH-ubiquinone oxidoreductase subunit; TC 2.A.63.1. (575 aa)
ABI65383.1PFAM: NADPH-dependent FMN reductase; flavodoxin/nitric oxide synthase; KEGG: mfa:Mfla_1832 NADPH-dependent FMN reductase. (213 aa)
ABI65442.1TIGRFAM: cytochrome c oxidase, cbb3-type, subunit I; PFAM: cytochrome c oxidase, subunit I; KEGG: ccr:CC1401 cb-type cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (550 aa)
ABI65443.1TIGRFAM: cytochrome c oxidase, cbb3-type, subunit II; PFAM: cytochrome C oxidase, mono-heme subunit/FixO; KEGG: ccr:CC1402 cb-type cytochrome c oxidase subunit II. (252 aa)
ABI65445.1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (307 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. (122 aa)
nuoBNADH 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). (188 aa)
nuoCNADH 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. (200 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. (402 aa)
ABI65651.1KEGG: ccr:CC1950 NADH dehydrogenase I chain E; TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone), 24 kDa subunit. (221 aa)
ABI65652.1NADH 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. (437 aa)
ABI65653.1NADH 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. (699 aa)
ABI65656.1NADH 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. (203 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. (103 aa)
ABI65658.1KEGG: ccr:CC1939 NADH dehydrogenase I chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I), chain 5/L domain protein; NADH/Ubiquinone/plastoquinone (complex I). (712 aa)
ABI65659.1KEGG: ccr:CC1938 NADH dehydrogenase I chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (504 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. (480 aa)
msrQFerric reductase domain protein transmembrane component, N-terminal domain; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduct [...] (224 aa)
ABI65788.1PFAM: ETC complex I subunit conserved region; KEGG: ccr:CC1389 NADH-ubiquinone oxidoreductase-related protein. (101 aa)
ABI65936.1SMART: Parallel beta-helix repeat; KEGG: ade:Adeh_2620 parallel beta-helix repeat protein. (423 aa)
ABI65955.1TIGRFAM: pseudoazurin; PFAM: blue (type 1) copper domain protein; KEGG: atc:AGR_L_2859 hypothetical protein. (153 aa)
ABI66058.1KEGG: mlo:mll3904 hypothetical protein. (124 aa)
ABI66127.1PFAM: cytochrome c, class I; KEGG: ccr:CC1210 cytochrome c family protein. (166 aa)
ABI66189.1KEGG: pub:SAR11_0982 hypothetical protein. (202 aa)
ABI66271.1KEGG: ade:Adeh_2620 parallel beta-helix repeat protein. (411 aa)
ABI66272.1KEGG: ade:Adeh_2621 hypothetical protein. (374 aa)
ABI66290.1KEGG: ccr:CC0714 membrane protein, putative. (410 aa)
ABI66480.1Electron-transferring-flavoprotein dehydrogenase; Accepts electrons from ETF and reduces ubiquinone. (557 aa)
ABI66521.1PFAM: cytochrome c oxidase, subunit III; KEGG: ccr:CC3402 cytochrome c oxidase, subunit III. (284 aa)
ABI66525.1Cytochrome-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. (544 aa)
ABI66526.1Cytochrome-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). (292 aa)
ABI66587.14Fe-4S ferredoxin, iron-sulfur binding domain protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (113 aa)
ABI66655.1PFAM: electron transfer flavoprotein beta-subunit; KEGG: ret:RHE_PF00405 electron transport flavoprotein, beta subunit. (249 aa)
ABI66656.1PFAM: electron transfer flavoprotein beta-subunit; electron transfer flavoprotein, alpha subunit; KEGG: rpa:RPA4749 electron transfer flavoprotein alpha-subunit, (ETFLS). (309 aa)
azoR(Acyl-carrier-protein) phosphodiesterase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (202 aa)
ABI66968.1PFAM: NADH dehydrogenase (ubiquinone), 24 kDa subunit; KEGG: bja:bll3138 NADH dehydrogenase I chain E. (163 aa)
ABI66969.1PFAM: Respiratory-chain NADH dehydrogenase domain, 51 kDa subunit; KEGG: reu:Reut_A0618 NADH dehydrogenase (quinone). (511 aa)
ABI66970.1TIGRFAM: formate dehydrogenase, alpha subunit; PFAM: ferredoxin; 4Fe-4S ferredoxin, iron-sulfur binding domain protein; molybdopterin oxidoreductase; molydopterin dinucleotide-binding region; molybdopterin oxidoreductase Fe4S4 region; KEGG: mfa:Mfla_0720 formate dehydrogenase, alpha subunit. (951 aa)
ABI67125.1TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; KEGG: sil:SPO0361 succinate dehydrogenase, iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa)
ABI67127.1KEGG: ccr:CC3527 succinate dehydrogenase, flavoprotein subunit; TIGRFAM: succinate dehydrogenase, flavoprotein subunit; succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; FAD dependent oxidoreductase; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (595 aa)
ABI67129.1PFAM: succinate dehydrogenase, cytochrome b subunit; KEGG: nha:Nham_3616 succinate dehydrogenase, cytochrome b subunit. (130 aa)
Your Current Organism:
Maricaulis maris
NCBI taxonomy Id: 394221
Other names: M. maris MCS10, Maricaulis maris MCS10, Maricaulis maris str. MCS10, Maricaulis maris strain MCS10
Server load: low (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.