KEGG   PATHWAY: awd00270
Entry
awd00270                    Pathway                                
Name
Cysteine and methionine metabolism - Aliivibrio wodanis
Description
Cysteine and methionine are sulfur-containing amino acids. Cysteine is synthesized from serine through different pathways in different organism groups. In bacteria and plants, cysteine is converted from serine (via acetylserine) by transfer of hydrogen sulfide [MD:M00021]. In animals, methionine-derived homocysteine is used as sulfur source and its condensation product with serine (cystathionine) is converted to cysteine [MD:M00338]. Cysteine is metabolized to pyruvate in multiple routes. Methionine is an essential amino acid, which animals cannot synthesize. In bacteria and plants, methionine is synthesized from aspartate [MD:M00017]. S-Adenosylmethionine (SAM), synthesized from methionine and ATP, is a methyl group donor in many important transfer reactions including DNA methylation for regulation of gene expression. SAM may also be used to regenerate methionine in the methionine salvage pathway [MD:M00034].
Class
Metabolism; Amino acid metabolism
Pathway map
awd00270  Cysteine and methionine metabolism
awd00270

Module
awd_M00017  Methionine biosynthesis, aspartate => homoserine => methionine [PATH:awd00270]
awd_M00021  Cysteine biosynthesis, serine => cysteine [PATH:awd00270]
Other DBs
GO: 0006534 0006555
Organism
Aliivibrio wodanis [GN:awd]
Gene
AWOD_I_0254  cysE; serine acetyltransferase [KO:K00640] [EC:2.3.1.30]
AWOD_I_2013  cysK; cysteine synthase A [KO:K01738] [EC:2.5.1.47]
AWOD_I_1675  putative pyridoxal-phosphate dependent enzyme [KO:K01738] [EC:2.5.1.47]
AWOD_I_1173  metC; cystathionine beta-lyase [KO:K01760] [EC:4.4.1.13]
AWOD_I_2336  metH; methionine synthase [KO:K00548] [EC:2.1.1.13]
AWOD_I_1844  metE; 5-methyltetrahydropteroyltriglutamate--homocyst eine methyltransferase [KO:K00549] [EC:2.1.1.14]
AWOD_I_2246  metK; S-adenosylmethionine synthetase [KO:K00789] [EC:2.5.1.6]
AWOD_I_1040  ainS; autoinducer synthase [KO:K13062] [EC:2.3.1.184]
AWOD_I_0467  mtnN; 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase [KO:K01243] [EC:3.2.2.9]
AWOD_I_0546  putative uncharacterized protein [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]
AWOD_I_1145  putative amidohydrolase [KO:K12960] [EC:3.5.4.31 3.5.4.28]
AWOD_I_1577  aspC; aspartate aminotransferase [KO:K00832] [EC:2.6.1.57]
AWOD_I_1392  putative uncharacterized protein [KO:K08968] [EC:1.8.4.14]
AWOD_I_0523  luxS; S-ribosylhomocysteine lyase [KO:K07173] [EC:4.4.1.21]
AWOD_I_1094  putative uncharacterized protein [KO:K01505] [EC:3.5.99.7]
AWOD_I_0514  lysC; aspartokinase [KO:K00928] [EC:2.7.2.4]
AWOD_II_1285  aspartokinase [KO:K00928] [EC:2.7.2.4]
AWOD_I_2335  lysC; aspartokinase [KO:K00928] [EC:2.7.2.4]
AWOD_I_2198  thrA; bifunctional aspartokinase/homoserine dehydrogenase I [KO:K12524] [EC:2.7.2.4 1.1.1.3]
AWOD_I_0336  metL; bifunctional aspartokinase/homoserine dehydrogenase II [KO:K12525] [EC:2.7.2.4 1.1.1.3]
AWOD_I_1767  aspartate-semialdehyde dehydrogenase [KO:K00133] [EC:1.2.1.11]
AWOD_I_1816  asd; aspartate-semialdehyde dehydrogenase [KO:K00133] [EC:1.2.1.11]
AWOD_I_2140  metA; homoserine O-succinyltransferase [KO:K00651] [EC:2.3.1.46 2.3.1.31]
AWOD_I_0335  metB; cystathionine gamma-synthase (O-succinylhomoserin (thiol)-lyase) [KO:K01739] [EC:2.5.1.48]
AWOD_I_0521  gshA; glutamate--cysteine ligase [KO:K01919] [EC:6.3.2.2]
AWOD_I_2130  putative glutathione synthetase [KO:K01920] [EC:6.3.2.3]
AWOD_I_2250  gshB; glutathione synthetase [KO:K01920] [EC:6.3.2.3]
AWOD_II_0297  amino acid biosynthesis aminotransferase [KO:K00813] [EC:2.6.1.1]
AWOD_I_1256  sulfurtransferase (rhodanese-like protein) [KO:K01011] [EC:2.8.1.1 2.8.1.2]
AWOD_I_0706  alr; alanine racemase [KO:K25317] [EC:5.1.1.10]
AWOD_I_2402  mdh; malate dehydrogenase [KO:K00024] [EC:1.1.1.37]
AWOD_I_1164  sdaA; L-serine dehydratase 1 [KO:K01752] [EC:4.3.1.17]
AWOD_II_1157  sdaA; L-serine dehydratase [KO:K01752] [EC:4.3.1.17]
AWOD_I_2187  serA; D-3-phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]
AWOD_I_0881  serC; phosphoserine aminotransferase [KO:K00831] [EC:2.6.1.52]
Compound
C00019  S-Adenosyl-L-methionine
C00021  S-Adenosyl-L-homocysteine
C00022  Pyruvate
C00041  L-Alanine
C00049  L-Aspartate
C00051  Glutathione
C00059  Sulfate
C00065  L-Serine
C00073  L-Methionine
C00094  Sulfite
C00097  L-Cysteine
C00109  2-Oxobutanoate
C00155  L-Homocysteine
C00170  5'-Methylthioadenosine
C00197  3-Phospho-D-glycerate
C00263  L-Homoserine
C00283  Hydrogen sulfide
C00409  Methanethiol
C00441  L-Aspartate 4-semialdehyde
C00491  L-Cystine
C00506  L-Cysteate
C00606  3-Sulfino-L-alanine
C00793  D-Cysteine
C00957  Mercaptopyruvate
C00979  O-Acetyl-L-serine
C01005  O-Phospho-L-serine
C01077  O-Acetyl-L-homoserine
C01118  O-Succinyl-L-homoserine
C01137  S-Adenosylmethioninamine
C01180  4-Methylthio-2-oxobutanoic acid
C01234  1-Aminocyclopropane-1-carboxylate
C01817  L-Homocystine
C01962  Thiocysteine
C02218  Dehydroalanine
C02291  L-Cystathionine
C02356  (S)-2-Aminobutanoate
C02989  L-Methionine S-oxide
C03082  4-Phospho-L-aspartate
C03089  5-Methylthio-D-ribose
C03145  N-Formylmethionine
C03232  3-Phosphonooxypyruvate
C03431  S-Inosyl-L-homocysteine
C03539  S-Ribosyl-L-homocysteine
C04188  S-Methyl-5-thio-D-ribose 1-phosphate
C04582  S-Methyl-5-thio-D-ribulose 1-phosphate
C05324  Nicotianamine
C05524  Aminoacyl-L-methionine
C05526  S-Glutathionyl-L-cysteine
C05527  3-Sulfinylpyruvate
C05528  3-Sulfopyruvate
C05823  3-Mercaptolactate
C05824  S-Sulfo-L-cysteine
C06547  Ethylene
C08276  3-(Methylthio)propanoate
C09306  Sulfur dioxide
C11437  1-Deoxy-D-xylulose 5-phosphate
C11481  HSO3-
C11499  (S)-3-Sulfolactate
C11537  (2R)-3-Sulfolactate
C15606  1,2-Dihydroxy-5-(methylthio)pent-1-en-3-one
C15650  2,3-Diketo-5-methylthiopentyl-1-phosphate
C15651  2-Hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
C18049  N-Acyl-L-homoserine lactone
C19787  5'-S-Methyl-5'-thioinosine
C21015  gamma-L-Glutamyl-L-2-aminobutyrate
C21016  Ophthalmate
C22359  S-Methyl-1-thio-D-xylulose 5-phosphate
Reference
  Authors
Sekowska A, Denervaud V, Ashida H, Michoud K, Haas D, Yokota A, Danchin A
  Title
Bacterial variations on the methionine salvage pathway.
  Journal
BMC Microbiol 4:9 (2004)
DOI:10.1186/1471-2180-4-9
Reference
  Authors
Ashida H, Saito Y, Kojima C, Kobayashi K, Ogasawara N, Yokota A.
  Title
A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO.
  Journal
Science 302:286-90 (2003)
DOI:10.1126/science.1086997
Reference
  Authors
Sekowska A, Danchin A.
  Title
The methionine salvage pathway in Bacillus subtilis.
  Journal
BMC Microbiol 2:8 (2002)
DOI:10.1186/1471-2180-2-8
Reference
  Authors
Berger BJ, English S, Chan G, Knodel MH.
  Title
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis.
  Journal
J Bacteriol 185:2418-31 (2003)
DOI:10.1128/JB.185.8.2418-2431.2003
Reference
  Authors
Goyer A, Collakova E, Shachar-Hill Y, Hanson AD
  Title
Functional characterization of a methionine gamma-lyase in Arabidopsis and its implication in an alternative to the reverse trans-sulfuration pathway.
  Journal
Plant Cell Physiol 48:232-42 (2007)
DOI:10.1093/pcp/pcl055
Reference
  Authors
Rebeille F, Jabrin S, Bligny R, Loizeau K, Gambonnet B, Van Wilder V, Douce R, Ravanel S
  Title
Methionine catabolism in Arabidopsis cells is initiated by a gamma-cleavage process and leads to S-methylcysteine and isoleucine syntheses.
  Journal
Proc Natl Acad Sci U S A 103:15687-92 (2006)
DOI:10.1073/pnas.0606195103
Reference
  Authors
Pirkov I, Norbeck J, Gustafsson L, Albers E
  Title
A complete inventory of all enzymes in the eukaryotic methionine salvage pathway.
  Journal
FEBS J 275:4111-20 (2008)
DOI:10.1111/j.1742-4658.2008.06552.x
Reference
  Authors
Ashida H, Saito Y, Kojima C, Yokota A
  Title
Enzymatic characterization of 5-methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway in Bacillus subtilis.
  Journal
Biosci Biotechnol Biochem 72:959-67 (2008)
DOI:10.1271/bbb.70651
Reference
  Authors
Kitabatake M, So MW, Tumbula DL, Soll D
  Title
Cysteine biosynthesis pathway in the archaeon Methanosarcina barkeri encoded by acquired bacterial genes?
  Journal
J Bacteriol 182:143-5 (2000)
DOI:10.1128/JB.182.1.143-145.2000
Reference
  Authors
Mino K, Ishikawa K
  Title
Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
  Journal
J Bacteriol 185:2277-84 (2003)
DOI:10.1128/JB.185.7.2277-2284.2003
Reference
  Authors
Tanabe S
  Title
Development of assay methods for endogenous inorganic sulfur compounds and sulfurtransferases and evaluation of the physiological functions of bound sulfur.
  Journal
Yakugaku Zasshi 128:881-900 (2008)
DOI:10.1248/yakushi.128.881
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
Gutierrez JA, Crowder T, Rinaldo-Matthis A, Ho MC, Almo SC, Schramm VL
  Title
Transition state analogs of 5'-methylthioadenosine nucleosidase disrupt quorum sensing.
  Journal
Nat Chem Biol 5:251-7 (2009)
DOI:10.1038/nchembio.153
Related
pathway
awd00010  Glycolysis / Gluconeogenesis
awd00250  Alanine, aspartate and glutamate metabolism
awd00260  Glycine, serine and threonine metabolism
awd00290  Valine, leucine and isoleucine biosynthesis
awd00430  Taurine and hypotaurine metabolism
awd00480  Glutathione metabolism
awd00620  Pyruvate metabolism
awd00640  Propanoate metabolism
awd00770  Pantothenate and CoA biosynthesis
awd00900  Terpenoid backbone biosynthesis
awd00920  Sulfur metabolism
KO pathway
ko00270   
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