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:
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[Homology]
Score
rutEMalonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. (196 aa)    
Predicted Functional Partners:
rutD
Aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in the pyrimidine nitrogen degradation. Belongs to the AB hydrolase superfamily. Hydrolase RutD family.
 
 
 0.992
rutA
Pyrimidine monooxygenase; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate.
 
  
 0.941
rutB
Amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2; Belongs to the isochorismatase family. RutB subfamily.
 
  
 0.931
rutF
FMN reductase; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway; Belongs to the non-flavoprotein flavin reductase family. RutF subfamily.
  
  
 0.923
ydfG_1
Malonic semialdehyde reductase; NADP(+)-dependent; catalyzes the formation of 3-hydroxypropionate from the toxic malonic semialdehyde, catalyzes the formation of 2-aminomalonate-semialdehyde from L-serine; can also use 3-hydroxybutyrate, 3-hydroxy-isobutyrate, D-threonine, L-allo-threonine,D-serine; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
  
 
 0.922
rutC
Aminoacrylate peracid reductase; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce by the pyrimidine nitrogen degradation.
  
  
 0.919
AKL36996.1
Pyrimidine permease; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.851
yecD
Hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.664
birA
biotin--[acetyl-CoA-carboxylase] synthetase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.
  
    0.656
AKL37226.1
Ribosomal protein S12 methylthiotransferase accessory factor YcaO; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.620
Your Current Organism:
Klebsiella oxytoca
NCBI taxonomy Id: 571
Other names: ATCC 13182, Bacillus oxytocus perniciosus, CCUG 15717, CIP 103434, DSM 5175, IAM 14201, K. oxytoca, Klebsiella sp. CECRI-24/07, Klebsiella sp. MN9SED2, LMG 3055, LMG:3055, NBRC 102593, NBRC 105695, NCTC 13727, strain 479-2
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