STRINGSTRING
BN938_0865 BN938_0865 adk adk BN938_1208 BN938_1208 guaB guaB BN938_1643 BN938_1643 tmk tmk BN938_1675 BN938_1675 BN938_1741 BN938_1741 gmk gmk guaA guaA BN938_2216 BN938_2216 ndk ndk surE surE BN938_2877 BN938_2877
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:
BN938_0865GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. (738 aa)
adkAdenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family. (192 aa)
BN938_1208GTP pyrophosphokinaseppGpp synthetase I; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. (708 aa)
guaBInosine-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. (490 aa)
BN938_1643Hypoxanthine-guanine phosphoribosyltransferase. (199 aa)
tmkThymidylate kinase; Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis; Belongs to the thymidylate kinase family. (217 aa)
BN938_1675Nucleoside 5-triphosphatase RdgB (dHAPTP, dITP,XTP-specific); Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. (195 aa)
BN938_1741Guanylate kinase. (177 aa)
gmkGuanylate kinase; Essential for recycling GMP and indirectly, cGMP. (191 aa)
guaAGMP synthase, glutamine-hydrolyzing; Catalyzes the synthesis of GMP from XMP. (509 aa)
BN938_2216Exopolyphosphatase. (297 aa)
ndkNucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family. (155 aa)
surE5-nucleotidase SurE; Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates; Belongs to the SurE nucleotidase family. (281 aa)
BN938_2877Ribonucleotide reductase of class II (coenzyme B12-dependent); Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen. (857 aa)
Your Current Organism:
Mucinivorans hirudinis
NCBI taxonomy Id: 1433126
Other names: ATCC BAA-2553, DSM 27344, M. hirudinis, Mucinivorans hirudinis Nelson et al. 2015, Rikenellaceae bacterium M3, Rikenellaceae bacterium M4, Rikenellaceae bacterium M6, strain M3
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