STRINGSTRING
pdxH pdxH AHW62739.1 AHW62739.1 AHW63083.1 AHW63083.1 AHW63398.1 AHW63398.1 AHW63479.1 AHW63479.1 ppx2 ppx2 AHW63849.1 AHW63849.1 AHW63997.1 AHW63997.1 AHW63999.1 AHW63999.1 pgsA2 pgsA2 AHW64001.1 AHW64001.1 AHW64002.1 AHW64002.1 AHW64003.1 AHW64003.1 AHW64004.1 AHW64004.1 AHW64065.1 AHW64065.1 pgsA1 pgsA1 AHW64067.1 AHW64067.1 pimA pimA AHW64069.1 AHW64069.1 pdxS pdxS tesB tesB pdxT pdxT AHW64073.1 AHW64073.1 AHW64074.1 AHW64074.1 ruvC ruvC ruvA ruvA ruvB ruvB secD secD secF secF AHW64081.1 AHW64081.1 relA relA
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:
pdxHPutative pyridoxine/pyridoxamine 5-phosphate oxidase. (194 aa)
AHW62739.1Hypothetical protein. (186 aa)
AHW63083.1Putative exopolyphosphatase, Ppx/GppA-family. (322 aa)
AHW63398.1Putative membrane protein. (1025 aa)
AHW63479.1Hypothetical protein. (201 aa)
ppx2Putative exopolyphosphatase. (319 aa)
AHW63849.1Hypothetical protein. (405 aa)
AHW63997.1Hypothetical protein. (204 aa)
AHW63999.1Putative membrane protein. (347 aa)
pgsA2Phosphatidylglycerophosphate synthase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. (221 aa)
AHW64001.1Putative secreted protein; Belongs to the CinA family. (192 aa)
AHW64002.1Putative transcriptional regulator, HTH3-family. (125 aa)
AHW64003.135 kDa protein. (282 aa)
AHW64004.1Hypothetical protein. (242 aa)
AHW64065.1Hypothetical protein; Catabolizes diadenosine 5',5'''-P1,P4- tetraphosphate (Ap4A) into ADP and ATP. It does not catalyze the reverse phosphorolysis reaction. The optimum substrates are dinucleoside polyphosphates containing four or five phosphate residues. (104 aa)
pgsA1Phosphatidylglycerophosphate synthase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. (252 aa)
AHW64067.1Lipid A biosynthesis lauroyl acyltransferase; Catalyzes the acylation to the position 6 of the alpha- 1,2-linked mannose residue of the phosphatidyl- myo-inositol dimannoside (PIM2) or monomannoside (PIM1). (315 aa)
pimAGDP-mannose-dependent alpha-(1-2)-phosphatidylinositol mannosyltransferase; Catalyzes the addition of a mannose residue from GDP-D- mannose to the position 2 of a phosphatidyl- myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Contrary to pimB, the mannosyltransferase pi. (384 aa)
AHW64069.1Putative membrane protein. (158 aa)
pdxSPyridoxal biosynthesis lyase PdxS; Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5- phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Belongs to the PdxS/SNZ family. (302 aa)
tesBAcyl-CoA thioesterase II. (300 aa)
pdxTGlutamine amidotransferase subunit PdxT; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. (218 aa)
AHW64073.1Putative transcriptional regulator. (250 aa)
AHW64074.1Putative membrane protein. (147 aa)
ruvCCrossover junction endodeoxyribonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. (178 aa)
ruvAHolliday junction ATP-dependent DNA helicase RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. (205 aa)
ruvBHolliday junction ATP-dependent DNA helicase RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. (355 aa)
secDProtein translocase subunit SecD; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (609 aa)
secFProtein translocase subunit SecF; Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. (413 aa)
AHW64081.1ABC-type peptide transporter, substrate binding lipoprotein. (605 aa)
relAGTP 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. (756 aa)
Your Current Organism:
Corynebacterium glyciniphilum
NCBI taxonomy Id: 1404245
Other names: C. glyciniphilum AJ 3170, Corynebacterium glyciniphilum AJ 3170, Corynebacterium glyciniphilum ATCC 21341, Corynebacterium glyciniphilum DSM 45795
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