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STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ADU46707.1TspO/MBR family protein; COGs: COG0702 nucleoside-diphosphate-sugar epimerase; InterPro IPR001509: IPR004307; KEGG: krh:KRH_21230 hypothetical protein; PFAM: TspO/MBR family protein; NAD-dependent epimerase/dehydratase; SPTR: Putative uncharacterized protein; PFAM: TspO/MBR family; NmrA-like family. (491 aa)    
Predicted Functional Partners:
acpP
Phosphopantetheine-binding protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family.
   
 0.968
ADU46709.1
COGs: COG0415 Deoxyribodipyrimidine photolyase; InterProIPR006050: IPR005101: IPR001969: IPR018394: IPR 002081; KEGG: kra:Krad_3554 deoxyribodipyrimidine photo-lyase; PFAM: DNA photolyase FAD-binding; DNA photolyase domain protein; PRIAM: Deoxyribodipyrimidine photo-lyase; SPTR: Phr; PFAM: FAD binding domain of DNA photolyase; DNA photolyase.
 
  
 0.963
nuoI
NADH 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.
   
 0.952
nuoI-2
4Fe-4S ferredoxin iron-sulfur binding domain protein; 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.
   
 0.952
nuoC
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 a menaquinone. 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.
   
 0.905
ADU47256.1
COGs: COG0852 NADH:ubiquinone oxidoreductase 27 kD subunit; InterPro IPR001268; KEGG: tcu:Tcur_4386 NADH (or F420H2) dehydrogenase, subunit C; PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; SPTR: Putative NADH dehydrogenase; PFAM: Respiratory-chain NADH dehydrogenase, 30 Kd subunit.
   
 0.905
ADU46997.1
FAD dependent oxidoreductase; COGs: COG0665 Glycine/D-amino acid oxidase (deaminating); InterPro IPR017941: IPR006076; KEGG: nda:Ndas_1353 FAD dependent oxidoreductase; PFAM: FAD dependent oxidoreductase; Rieske [2Fe-2S] iron-sulphur domain; SPTR: FAD dependent oxidoreductase; PFAM: Rieske [2Fe-2S] domain; FAD dependent oxidoreductase.
  
 
 0.904
nuoD
NADH 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 a menaquinone. 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.
   
 0.900
nuoD-2
NADH 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 a menaquinone. 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.
   
 0.900
nuoB
NADH 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 a menaquinone. 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.
   
 0.882
Your Current Organism:
Intrasporangium calvum
NCBI taxonomy Id: 710696
Other names: I. calvum DSM 43043, Intrasporangium calvum DSM 43043, Intrasporangium calvum IFO 12989, Intrasporangium calvum NBRC 12989, Intrasporangium calvum str. DSM 43043, Intrasporangium calvum strain DSM 43043
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