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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
rppHProbable (di)nucleoside polyphosphate hydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily. (175 aa)    
Predicted Functional Partners:
nadE
NAD(+) synthase (glutamine-hydrolyzing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
    
 0.704
metH
Probable methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
    
 0.662
azo0728
Bifunctional DGTP-pyrophosphohydrolase/Thiamine-phosphate diphosphorylase; NUDIX hydrolase/thiamine phosphate synthase Condenses 4-methyl-5-(beta-hydroxyethyl)-thiazole monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP) (By similarity). InterPro: NUDIX hydrolase TIGRFAM: mutt: mutator mutT protein; High confidence in function and specificity.
  
 
 0.645
azo2763
Conserved hypothetical secreted protein. Homology to ebA945 of Azoarcus sp. EbN1 of 47% (gnl|keqq|eba:ebA945(KEGG)). No domains predicted. Signal P reporting signal peptide present. No TMH present; Conserved hypothetical protein.
       0.616
fumB
Putative fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
    
  0.609
coq7
Ubiquinone biosynthesis protein; Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6- methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
       0.596
ribAB
GTP cyclohydrolase II; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; Belongs to the DHBP synthase family.
     
  0.581
proS
Proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...]
       0.575
azo0628
Putative adenylate/guanylate cyclase,; Conserved hypothetical protein.
     
  0.553
azo0484
FHA domain containing protein. Best similarity to SWISSPROT: sprot|REPB_AGRRH (9% Agrobacterium rhizogenes,possible replication protein b) Pfam: PF00211 Adenylate and Guanylate cyclase catalytic domain. SMART: SM00240 FHA Forkhead associated domain.
     
  0.526
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.