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
ALV29505.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (565 aa)    
Predicted Functional Partners:
ALV27063.1
Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.847
ALV27716.1
Nitrite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
  
 
 0.847
ALV27847.1
Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.847
ALV26005.1
Siroheme synthase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. Belongs to the precorrin methyltransferase family. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
  
  
 0.846
ALV27718.1
Siroheme synthase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. Belongs to the precorrin methyltransferase family. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
  
  
 0.846
ALV29504.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.779
narH
Nitrate reductase; With NarGJI catalyzes the reduction of nitrate; the beta subunit is an iron sulfur cluster containing electron transfer subunit; one of 3 nitrate reductases in E. coli and in E. coli is expressed when nitrate levels are high; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.706
ALV28463.1
Sarcosine oxidase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GcvT family.
  
 
 0.688
ALV29225.1
Sarcosine oxidase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the GcvT family.
  
 
 0.688
hemN_1
Coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family.
 
     0.673
Your Current Organism:
Pannonibacter phragmitetus
NCBI taxonomy Id: 121719
Other names: Achromobacter group B, Achromobacter group E, Achromobacter sp. LMG 5410, Achromobacter sp. LMG 5411, Achromobacter sp. LMG 5430, Achromobacter sp. LMG 5431, DSM 14782, LMG 22736, LMG:22736, NCAIM B02025, NCTC 13350, P. phragmitetus, Pannonibacter phragmitetus Borsodi et al. 2003, alpha proteobacterium C6-19, alpha proteobacterium C6/17, alpha proteobacterium C6/8, strain C6/19
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