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
ADQ79514.1Diaminohydroxyphosphoribosylaminopyrimidine deaminase; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- phosphate; In the C-terminal section; belongs to the HTP reductase family. (360 aa)    
Predicted Functional Partners:
ribBA
3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
 0.999
ADQ79621.1
COGs: COG0307 Riboflavin synthase alpha chain; InterPro IPR001783; KEGG: bth:BT_1317 riboflavin synthase subunit alpha; PFAM: Lumazine-binding protein; PRIAM: Riboflavin synthase; SPTR: Riboflavin synthase alpha chain; TIGRFAM: riboflavin synthase, alpha subunit; PFAM: Lumazine binding domain; TIGRFAM: riboflavin synthase, alpha subunit.
  
 0.998
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
 
 0.986
ADQ80510.1
Bifunctional deaminase-reductase domain protein; COGs: COG1985 Pyrimidine reductase riboflavin biosynthesis; KEGG: kfl:Kfla_3159 bifunctional deaminase-reductase domain protein; SPTR: Bifunctional deaminase-reductase domain protein; PFAM: RibD C-terminal domain.
    
  0.906
ADQ79302.1
Protein of unknown function DUF201; COGs: COG0439 Biotin carboxylase; InterPro IPR011761: IPR003806; KEGG: cbk:CLL_A3240 putative carbamoyl-phosphate synthase large chain; PFAM: protein of unknown function DUF201; SPTR: Putative carbamoyl-phosphate synthase; manually curated; PFAM: D-ala D-ala ligase C-terminus.
   
   0.869
ADQ79513.1
Phospholipase D/Transphosphatidylase; Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
     
 0.758
nadD
Nicotinate (nicotinamide) nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
 
  
 0.688
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
  
  
 0.678
ADQ80886.1
Riboflavin biosynthesis protein RibF; COGs: COG0196 FAD synthase; InterPro IPR002606: IPR015864: IPR015865; KEGG: bfr:BF4346 putative riboflavin kinase; PFAM: Riboflavin kinase; FAD synthetase; SPTR: Putative riboflavin kinase; TIGRFAM: riboflavin biosynthesis protein RibF; PFAM: Riboflavin kinase; FAD synthetase; TIGRFAM: riboflavin kinase/FMN adenylyltransferase; Belongs to the ribF family.
 
  
 0.666
nadE
NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
  
  
 0.656
Your Current Organism:
Paludibacter propionicigenes
NCBI taxonomy Id: 694427
Other names: P. propionicigenes WB4, Paludibacter propionicigenes CCUG 53888, Paludibacter propionicigenes DSM 17365, Paludibacter propionicigenes JCM 13257, Paludibacter propionicigenes WB4, Paludibacter propionicigenes str. WB4, Paludibacter propionicigenes strain WB4
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