STRINGSTRING
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
Oant_2407Methylmalonyl-CoA epimerase; PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase; KEGG: bmb:BruAb1_0832 glyoxalase family protein. (134 aa)    
Predicted Functional Partners:
Oant_2001
TIGRFAM: methylmalonyl-CoA mutase, large subunit; PFAM: methylmalonyl-CoA mutase; cobalamin B12-binding domain protein; KEGG: bms:BR1190 methylmalonyl-CoA mutase.
 
  
 0.986
Oant_2003
PFAM: carboxyl transferase; KEGG: bmb:BruAb1_1193 propionlyl-CoA carboxylase.
 
 
 0.979
Oant_2002
Carbamoyl-phosphate synthase L chain ATP-binding; PFAM: biotin/lipoyl attachment domain-containing protein; ATP-dependent carboxylate-amine ligase domain protein ATP-grasp; Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain domain protein; biotin carboxylase domain protein; RimK domain protein ATP-grasp; KEGG: bms:BR1189 propionyl-CoA carboxylase, alpha subunit.
 
 
 0.921
Oant_2406
PFAM: protein of unknown function DUF1467; KEGG: bms:BR0819 hypothetical protein.
       0.800
Oant_2408
PFAM: beta-lactamase domain protein; RNA-metabolising metallo-beta-lactamase; KEGG: bms:BR0817 metallo-beta-lactamase family protein.
       0.692
nuoI
NADH-quinone oxidoreductase, chain 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.
  
  
 0.647
Oant_2409
TIGRFAM: biotin--acetyl-CoA-carboxylase ligase; PFAM: biotin protein ligase domain protein; biotin/lipoate A/B protein ligase; KEGG: bms:BR0816 biotin--acetyl-CoA-carboxylase ligase.
  
    0.580
nuoD
NADH dehydrogenase I, D subunit; 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.
  
    0.561
Oant_2412
TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; NADH/Ubiquinone/plastoquinone (complex I); NADH dehydrogenase subunit 5 domain protein; KEGG: bme:BMEI1147 NADH-quinone oxidoreductase chain L.
  
    0.505
nuoN
Proton-translocating NADH-quinone oxidoreductase, chain 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.
       0.494
Your Current Organism:
Ochrobactrum anthropi
NCBI taxonomy Id: 439375
Other names: O. anthropi ATCC 49188, Ochrobactrum anthropi ATCC 49188, Ochrobactrum anthropi DSM 6882, Ochrobactrum anthropi LMG 3331, Ochrobactrum anthropi str. ATCC 49188, Ochrobactrum anthropi strain ATCC 49188
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