KEGG   PATHWAY: sinl00270
Entry
sinl00270                   Pathway                                
Name
Cysteine and methionine metabolism - Sulfitobacter indolifex
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
sinl00270  Cysteine and methionine metabolism
sinl00270

Module
sinl_M00017  Methionine biosynthesis, aspartate => homoserine => methionine [PATH:sinl00270]
sinl_M00021  Cysteine biosynthesis, serine => cysteine [PATH:sinl00270]
Other DBs
GO: 0006534 0006555
Organism
Sulfitobacter indolifex [GN:sinl]
Gene
DSM14862_01824  cysE; Serine acetyltransferase [KO:K00640] [EC:2.3.1.30]
DSM14862_01551  cysK; Cysteine synthase [KO:K01738] [EC:2.5.1.47]
DSM14862_02724  dcsD; O-ureido-L-serine synthase [KO:K01738] [EC:2.5.1.47]
DSM14862_03090  patB; Cystathionine beta-lyase PatB [KO:K14155] [EC:4.4.1.13]
DSM14862_01463  acsE; 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase [KO:K00548] [EC:2.1.1.13]
DSM14862_01588  metH_1; Methionine synthase [KO:K00548] [EC:2.1.1.13]
DSM14862_02326  metK; S-adenosylmethionine synthase [KO:K00789] [EC:2.5.1.6]
DSM14862_00831  mtnP; S-methyl-5'-thioadenosine phosphorylase [KO:K00772] [EC:2.4.2.28]
DSM14862_00702  yfiH; Polyphenol oxidase [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]
DSM14862_04007  mdeA; L-methionine gamma-lyase [KO:K01761] [EC:4.4.1.11]
DSM14862_00419  msrC; Free methionine-R-sulfoxide reductase [KO:K08968] [EC:1.8.4.14]
DSM14862_00106  ahcY; Adenosylhomocysteinase [KO:K01251] [EC:3.13.2.1]
DSM14862_03236  ask; Aspartate kinase Ask_Ect [KO:K00928] [EC:2.7.2.4]
DSM14862_00843  Aspartate kinase [KO:K00928] [EC:2.7.2.4]
DSM14862_00373  asd2; Aspartate-semialdehyde dehydrogenase 2 [KO:K00133] [EC:1.2.1.11]
DSM14862_01030  hom; Homoserine dehydrogenase [KO:K00003] [EC:1.1.1.3]
DSM14862_01370  metAA; Homoserine O-acetyltransferase [KO:K00651] [EC:2.3.1.46 2.3.1.31]
DSM14862_02009  metB; Cystathionine gamma-synthase [KO:K01739] [EC:2.5.1.48]
DSM14862_02136  mgl; L-methionine gamma-lyase [KO:K01740] [EC:2.5.1.49]
DSM14862_01055  metZ; O-succinylhomoserine sulfhydrylase [KO:K10764] [EC:2.5.1.-]
DSM14862_02459  ilvE_2; Branched-chain-amino-acid aminotransferase [KO:K00826] [EC:2.6.1.42]
DSM14862_00258  ilvE_1; Branched-chain-amino-acid aminotransferase [KO:K00826] [EC:2.6.1.42]
DSM14862_00617  egtA; Glutamate--cysteine ligase EgtA [KO:K01919] [EC:6.3.2.2]
DSM14862_02911  gshB; Glutathione synthetase [KO:K01920] [EC:6.3.2.3]
DSM14862_03574  aspB; Asparagine--oxo-acid transaminase [KO:K00812] [EC:2.6.1.1]
DSM14862_00954  Aspartate aminotransferase [KO:K00812] [EC:2.6.1.1]
DSM14862_00333  tyrB; Aromatic-amino-acid aminotransferase [KO:K00813] [EC:2.6.1.1]
DSM14862_00332  sseA; 3-mercaptopyruvate sulfurtransferase [KO:K01011] [EC:2.8.1.1 2.8.1.2]
DSM14862_02483  mdh_2; Malate dehydrogenase [KO:K00024] [EC:1.1.1.37]
DSM14862_01602  cuyA; L-cysteate sulfo-lyase [KO:K17950] [EC:4.4.1.25]
DSM14862_01034  tdcG; L-serine dehydratase TdcG [KO:K01752] [EC:4.3.1.17]
DSM14862_02076  Hydroxypyruvate reductase [KO:K00058] [EC:1.1.1.95 1.1.1.399]
DSM14862_03243  serA; D-3-phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]
DSM14862_03242  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
sinl00010  Glycolysis / Gluconeogenesis
sinl00250  Alanine, aspartate and glutamate metabolism
sinl00260  Glycine, serine and threonine metabolism
sinl00290  Valine, leucine and isoleucine biosynthesis
sinl00430  Taurine and hypotaurine metabolism
sinl00480  Glutathione metabolism
sinl00620  Pyruvate metabolism
sinl00640  Propanoate metabolism
sinl00770  Pantothenate and CoA biosynthesis
sinl00900  Terpenoid backbone biosynthesis
sinl00920  Sulfur metabolism
KO pathway
ko00270   
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