KEGG   PATHWAY: fno00260Help
Entry
fno00260                    Pathway                                
Name
Glycine, serine and threonine metabolism - Fervidobacterium nodosum
Description
Serine is derived from 3-phospho-D-glycerate, an intermediate of glycolysis [MD:M00020], and glycine is derived from serine. Threonine is an essential amino acid, which animals cannot synthesize. In bacteria and plants, threonine is derived from aspartate [MD:M00018].
Class
Metabolism; Amino acid metabolism
BRITE hierarchy
Pathway map
Glycine, serine and threonine metabolism
fno00260

All organismsOrtholog table
Module
Threonine biosynthesis, aspartate => homoserine => threonine [PATH:fno00260]
Serine biosynthesis, glycerate-3P => serine [PATH:fno00260]
Ectoine biosynthesis, aspartate => ectoine [PATH:fno00260]
Betaine biosynthesis, choline => betaine [PATH:fno00260]
Other DBs
Organism
Fervidobacterium nodosum [GN:fno]
Gene
aspartate kinase; K00928 aspartate kinase [EC:2.7.2.4] [KO:K00928] [EC:2.7.2.4]
aspartate kinase; K00928 aspartate kinase [EC:2.7.2.4] [KO:K00928] [EC:2.7.2.4]
aspartate-semialdehyde dehydrogenase; K00133 aspartate-semialdehyde dehydrogenase [EC:1.2.1.11] [KO:K00133] [EC:1.2.1.11]
glyA; serine hydroxymethyltransferase [KO:K00600] [EC:2.1.2.1]
phosphoglycerate dehydrogenase; K00058 D-3-phosphoglycerate dehydrogenase [EC:1.1.1.95] [KO:K00058] [EC:1.1.1.95]
phosphoglycerate mutase; K15634 probable phosphoglycerate mutase [EC:5.4.2.1] [KO:K15634] [EC:5.4.2.1]
cofactor-independent phosphoglycerate mutase; K15635 2,3-bisphosphoglycerate-independent phosphoglycerate mutase [EC:5.4.2.1] [KO:K15635] [EC:5.4.2.1]
hydroxypyruvate reductase; K00050 hydroxypyruvate reductase [EC:1.1.1.81] [KO:K00050] [EC:1.1.1.81]
pyridoxal phosphate-dependent acyltransferase; K00639 glycine C-acetyltransferase [EC:2.3.1.29] [KO:K00639] [EC:2.3.1.29]
alcohol dehydrogenase; K00060 threonine 3-dehydrogenase [EC:1.1.1.103] [KO:K00060] [EC:1.1.1.103]
glycine dehydrogenase subunit 1; K00282 glycine dehydrogenase subunit 1 [EC:1.4.4.2] [KO:K00282] [EC:1.4.4.2]
glycine dehydrogenase subunit 2; K00283 glycine dehydrogenase subunit 2 [EC:1.4.4.2] [KO:K00283] [EC:1.4.4.2]
gcvT; glycine cleavage system aminomethyltransferase T [KO:K00605] [EC:2.1.2.10]
dihydrolipoamide dehydrogenase; K00382 dihydrolipoamide dehydrogenase [EC:1.8.1.4] [KO:K00382] [EC:1.8.1.4]
FAD dependent oxidoreductase; K00303 sarcosine oxidase, subunit beta [EC:1.5.3.1] [KO:K00303] [EC:1.5.3.1]
L-serine dehydratase; K01752 L-serine dehydratase [EC:4.3.1.17] [KO:K01752] [EC:4.3.1.17]
L-serine dehydratase; K01752 L-serine dehydratase [EC:4.3.1.17] [KO:K01752] [EC:4.3.1.17]
tryptophan synthase subunit beta; K06001 tryptophan synthase beta chain [EC:4.2.1.20] [KO:K06001] [EC:4.2.1.20]
Compound
C00011  
CO2
C00014  
Ammonia
C00022  
Pyruvate
C00037  
Glycine
C00048  
Glyoxylate
C00049  
L-Aspartate
C00065  
L-Serine
C00078  
L-Tryptophan
C00097  
L-Cysteine
C00101  
Tetrahydrofolate
C00109  
2-Oxobutanoate
C00114  
Choline
C00143  
5,10-Methylenetetrahydrofolate
C00168  
Hydroxypyruvate
C00188  
L-Threonine
C00197  
3-Phospho-D-glycerate
C00213  
Sarcosine
C00258  
D-Glycerate
C00263  
L-Homoserine
C00300  
Creatine
C00430  
5-Aminolevulinate
C00441  
L-Aspartate 4-semialdehyde
C00546  
Methylglyoxal
C00576  
Betaine aldehyde
C00581  
Guanidinoacetate
C00631  
2-Phospho-D-glycerate
C00719  
Betaine
C00740  
D-Serine
C00986  
1,3-Diaminopropane
C01005  
O-Phospho-L-serine
C01026  
N,N-Dimethylglycine
C01102  
O-Phospho-L-homoserine
C01242  
S-Aminomethyldihydrolipoylprotein
C01726  
D-Lombricine
C01888  
Aminoacetone
C02051  
Lipoylprotein
C02291  
L-Cystathionine
C02737  
Phosphatidylserine
C02855  
N-Phospho-D-lombricine
C02972  
Dihydrolipoylprotein
C03082  
4-Phospho-L-aspartate
C03194  
(R)-1-Aminopropan-2-ol
C03232  
3-Phosphonooxypyruvate
C03283  
L-2,4-Diaminobutanoate
C03508  
L-2-Amino-3-oxobutanoic acid
C05235  
Hydroxyacetone
C05519  
L-Allothreonine
C06231  
Ectoine
C06442  
N-gamma-Acetyldiaminobutyrate
C16432  
5-Hydroxyectoine
C19929  
N-alpha-Acetyl-L-2,4-diaminobutyrate
Reference
  Authors
Nishizuka Y, Seyama Y, Ikai A, Ishimura Y, Kawaguchi A (eds).
  Title
[Cellular Functions and Metabolic Maps] (In Japanese)
  Journal
Tokyo Kagaku Dojin (1997)
Reference
  Authors
Kuhlmann AU, Bremer E.
  Title
Osmotically regulated synthesis of the compatible solute ectoine in Bacillus pasteurii and related Bacillus spp.
  Journal
Appl Environ Microbiol 68:772-83 (2002)
Reference
  Authors
Canovas D, Borges N, Vargas C, Ventosa A, Nieto JJ, Santos H.
  Title
Role of Ngamma-acetyldiaminobutyrate as an enzyme stabilizer and an intermediate in the biosynthesis of hydroxyectoine.
  Journal
Appl Environ Microbiol 65:3774-9 (1999)
Reference
  Authors
Bursy J, Pierik AJ, Pica N, Bremer E.
  Title
Osmotically induced synthesis of the compatible solute hydroxyectoine is mediated by an evolutionarily conserved ectoine hydroxylase.
  Journal
J Biol Chem 282:31147-55 (2007)
Reference
  Authors
Garcia-Estepa R, Argandona M, Reina-Bueno M, Capote N, Iglesias-Guerra F, Nieto JJ, Vargas C.
  Title
The ectD gene, which is involved in the synthesis of the compatible solute hydroxyectoine, is essential for thermoprotection of the halophilic bacterium Chromohalobacter salexigens.
  Journal
J Bacteriol 188:3774-84 (2006)
Reference
  Authors
Arevalo-Rodriguez M, Pan X, Boeke JD, Heitman J
  Title
FKBP12 controls aspartate pathway flux in Saccharomyces cerevisiae to prevent toxic intermediate accumulation.
  Journal
Eukaryot Cell 3:1287-96 (2004)
Reference
PMID:7639721
  Authors
Rees WD, Hay SM
  Title
The biosynthesis of threonine by mammalian cells: expression of a complete bacterial biosynthetic pathway in an animal cell.
  Journal
Biochem J 309 ( Pt 3):999-1007 (1995)
Reference
  Authors
Jacques SL, Nieman C, Bareich D, Broadhead G, Kinach R, Honek JF, Wright GD
  Title
Characterization of yeast homoserine dehydrogenase, an antifungal target: the invariant histidine 309 is important for enzyme integrity.
  Journal
Biochim Biophys Acta 1544:28-41 (2001)
Reference
  Authors
Chen X, Jhee KH, Kruger WD
  Title
Production of the neuromodulator H2S by cystathionine beta-synthase via the condensation of cysteine and homocysteine.
  Journal
J Biol Chem 279:52082-6 (2004)
KO pathway
 
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