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
pyrCDihydroorotase, multifunctional complex type; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate; Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily. (423 aa)    
Predicted Functional Partners:
pyrB
TIGRFAM: Aspartate carbamoyltransferase, eukaryotic; KEGG: cce:Ccel_0612 aspartate carbamoyltransferase catalytic subunit; PFAM: Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding; Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
 0.999
pyrD
Dihydroorotate dehydrogenase family protein; Catalyzes the conversion of dihydroorotate to orotate.
 
 0.998
carA
TIGRFAM: Carbamoyl-phosphate synthase, small subunit; KEGG: amt:Amet_4211 carbamoyl phosphate synthase small subunit; PFAM: Carbamoyl-phosphate synthase, small subunit, N-terminal; Glutamine amidotransferase class-I, C-terminal; Belongs to the CarA family.
  
 0.996
ADZ83539.1
PFAM: Dihydroorotate dehydrogenase, electron transfer subunit, iron-sulphur cluster binding domain; Oxidoreductase FAD/NAD(P)-binding; KEGG: amt:Amet_4209 oxidoreductase FAD/NAD(P)-binding subunit.
 
 
 0.996
carB
SMART: Methylglyoxal synthase-like domain; TIGRFAM: Carbamoyl-phosphate synthase, large subunit; KEGG: cdl:CDR20291_3426 carbamoyl phosphate synthase large subunit; PFAM: Carbamoyl-phosphate synthetase, large subunit, ATP-binding; Carbamoyl-phosphate synthetase, large subunit, oligomerisation; Methylglyoxal synthase-like domain; Carbamoyl-phosphate synthase, large subunit, N-terminal; Belongs to the CarB family.
 
 0.993
ADZ82015.1
SMART: Methylglyoxal synthase-like domain; TIGRFAM: Carbamoyl-phosphate synthase, large subunit; KEGG: bpb:bpr_I1679 carbamoyl-phosphate synthase large subunit CarB2; PFAM: Carbamoyl-phosphate synthetase, large subunit, ATP-binding; Carbamoyl-phosphate synthetase, large subunit, oligomerisation; Methylglyoxal synthase-like domain; Carbamoyl-phosphate synthase, large subunit, N-terminal; Belongs to the CarB family.
 
 0.986
pyrR
Uracil phosphoribosyltransferase; Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant; Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.
 
 
 0.969
pyrE
Orotate phosphoribosyltransferase; Catalyzes the transfer of a ribosyl phosphate group from 5- phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
  
  
 0.941
pyrF
SMART: Orotidine 5'-phosphate decarboxylase domain; TIGRFAM: Orotidine 5'-phosphate decarboxylase, type 2; KEGG: amt:Amet_4212 orotidine 5'-phosphate decarboxylase; PFAM: Orotidine 5'-phosphate decarboxylase domain; Belongs to the OMP decarboxylase family. Type 2 subfamily.
 
  
 0.936
ADZ83693.1
Uracil-xanthine permease; KEGG: cbe:Cbei_1715 uracil transporter; TIGRFAM: Xanthine/uracil permease; PFAM: Xanthine/uracil/vitamin C permease.
  
  
 0.914
Your Current Organism:
Cellulosilyticum lentocellum
NCBI taxonomy Id: 642492
Other names: C. lentocellum DSM 5427, Cellulosilyticum lentocellum DSM 5427, Clostridium lentocellum ATCC 49066, Clostridium lentocellum DSM 5427, Clostridium lentocellum str. DSM 5427, Clostridium lentocellum strain DSM 5427
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