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Information on Organism Caulobacter vibrioides NA1000

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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1-butanol autotrophic biosynthesis (engineered)
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PWY-6886
Bifidobacterium shunt
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P124-PWY
Biosynthesis of secondary metabolites
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citric acid cycle
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D-fructuronate degradation
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PWY-7242
d-xylose degradation
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D-xylose degradation III
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PWY-6760
D-xylose degradation V
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PWY-8020
D-xylose degradation VI
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PWY-8330
degradation of sugar acids
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Entner-Doudoroff pathway I
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PWY-8004
Entner-Doudoroff pathway II (non-phosphorylative)
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NPGLUCAT-PWY
Entner-Doudoroff pathway III (semi-phosphorylative)
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PWY-2221
ethene biosynthesis V (engineered)
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PWY-7124
formaldehyde assimilation I (serine pathway)
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PWY-1622
gluconeogenesis I
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GLUCONEO-PWY
gluconeogenesis II (Methanobacterium thermoautotrophicum)
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PWY-6142
gluconeogenesis III
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PWY66-399
glycerol degradation to butanol
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PWY-7003
glycolysis
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Glycolysis / Gluconeogenesis
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glycolysis I (from glucose 6-phosphate)
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GLYCOLYSIS
glycolysis II (from fructose 6-phosphate)
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PWY-5484
glycolysis III (from glucose)
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ANAGLYCOLYSIS-PWY
glycolysis IV
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PWY-1042
glycolysis V (Pyrococcus)
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P341-PWY
glyoxylate cycle
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GLYOXYLATE-BYPASS
heterolactic fermentation
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P122-PWY
Metabolic pathways
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Methane metabolism
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methylaspartate cycle
Microbial metabolism in diverse environments
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mixed acid fermentation
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FERMENTATION-PWY
nitrogen remobilization from senescing leaves
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PWY-6549
partial TCA cycle (obligate autotrophs)
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PWY-5913
Pentose and glucuronate interconversions
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peptidoglycan recycling I
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PWY0-1261
peptidoglycan recycling II
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PWY-7883
photosynthetic 3-hydroxybutanoate biosynthesis (engineered)
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PWY-7218
ppGpp biosynthesis
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ppGpp metabolism
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PPGPPMET-PWY
Purine metabolism
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Rubisco shunt
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PWY-5723
superpathway of glucose and xylose degradation
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PWY-6901
TCA cycle I (prokaryotic)
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TCA
TCA cycle II (plants and fungi)
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PWY-5690
TCA cycle III (animals)
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PWY66-398
TCA cycle IV (2-oxoglutarate decarboxylase)
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P105-PWY
TCA cycle V (2-oxoglutarate synthase)
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PWY-6969
TCA cycle VI (Helicobacter)
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REDCITCYC
TCA cycle VII (acetate-producers)
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PWY-7254
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the enzyme belongs to the divisome. AmiC recruitment to divisome is independent of endopeptidase DipM
0
Manually annotated by BRENDA team
additional information
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the amidase-3 family catalytic domain of AmiC is essential for medial localization
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0
Manually annotated by BRENDA team
LINKS TO OTHER DATABASES (specific for Caulobacter vibrioides NA1000)