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
glmMPhosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the phosphohexose mutase family. (445 aa)    
Predicted Functional Partners:
glmU
Glucosamine-1-phosphate N-acetyltransferase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain.
  
 0.985
folP
Dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
 
  
 0.960
glmS
Glucosamine--fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
 
 0.908
cpsB
Mannose-1-phosphate guanyltransferase; Capsular polysaccharide colanic acid biosynthesis protein; catalyzes the formation of GDP-mannose from GTP and alpha-D-mannose 1-phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the mannose-6-phosphate isomerase type 2 family.
 
 
 0.868
KMT64737.1
Alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.851
KMT65825.1
N-acetylglucosamine 6-phosphate deacetylase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the metallo-dependent hydrolases superfamily. NagA family.
     
 0.842
hflB
ATP-dependent metalloprotease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
 
  
 0.764
recA
Recombinase RecA; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
    
 0.756
KMT64928.1
Phosphoglucomutase; Catalyzes the interconversion of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
0.741
murC
UDP-N-acetylmuramate--alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
  
 
 
 0.733
Your Current Organism:
Catenovulum maritimum
NCBI taxonomy Id: 1513271
Other names: C. maritimum, CICC 10836, Catenovulum maritimum corrig. Li et al. 2016, Catenovulum maritimus, DSM 28813, Gammaproteobacteria bacterium Q1, Mariagarivorans maritimus, strain Q1
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