STRINGSTRING
nuoL nuoL nuoM nuoM nuoN nuoN dmsC_1 dmsC_1 dld dld cydA_1 cydA_1 fdnI fdnI APG52912.1 APG52912.1 ybgT ybgT cydA_2 cydA_2 APG52402.1 APG52402.1 dmsC_2 dmsC_2 fdoI fdoI cyoC cyoC nqrB_1 nqrB_1 nqrE nqrE yceJ yceJ nuoC nuoC nuoE nuoE nuoG nuoG nuoK nuoK
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:
nuoLNADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (618 aa)
nuoMNADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (506 aa)
nuoNNADH-quinone oxidoreductase 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. (487 aa)
dmsC_1Diguanylate cyclase; Derived by automated computational analysis using gene prediction method: Protein Homology. (258 aa)
dldD-lactate dehydrogenase; Catalyzes the oxidation of D-lactate to pyruvate. Belongs to the quinone-dependent D-lactate dehydrogenase family. (577 aa)
cydA_1Cytochrome D ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (445 aa)
fdnIFormate dehydrogenase subunit gamma; Derived by automated computational analysis using gene prediction method: Protein Homology. (217 aa)
APG52912.1Reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (300 aa)
ybgTCyd operon protein YbgT; Derived by automated computational analysis using gene prediction method: Protein Homology. (37 aa)
cydA_2Cytochrome d terminal oxidase subunit 1; Part of the aerobic respiratory chain; catalyzes the ubiquinol to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (522 aa)
APG52402.1Electron transfer flavoprotein-ubiquinone oxidoreductase; Accepts electrons from ETF and reduces ubiquinone. (560 aa)
dmsC_2Dimethylsulfoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (285 aa)
fdoIFormate dehydrogenase cytochrome b556 subunit; Cytochrome b556(FDO) component; heme containing; Derived by automated computational analysis using gene prediction method: Protein Homology. (216 aa)
cyoCCytochrome o ubiquinol oxidase subunit III; Derived by automated computational analysis using gene prediction method: Protein Homology. (204 aa)
nqrB_1NADH:ubiquinone reductase (Na(+)-transporting) subunit B; NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. (412 aa)
nqrENADH:ubiquinone reductase (Na(+)-transporting) subunit E; NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol; Belongs to the NqrDE/RnfAE family. (198 aa)
yceJDerived by automated computational analysis using gene prediction method: Protein Homology. (185 aa)
nuoCNADH-quinone oxidoreductase subunit C/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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. (598 aa)
nuoENADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. (180 aa)
nuoGNADH-quinone oxidoreductase 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. (910 aa)
nuoKNADH-quinone oxidoreductase 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. (100 aa)
Your Current Organism:
Providencia stuartii
NCBI taxonomy Id: 588
Other names: ATCC 29914, CCUG 14805, CDC 2896-68, CIP 104687, DSM 4539, LMG 3260, LMG:3260, NCTC 11800, P. stuartii, Proteus stuartii
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