KEGG   PATHWAY: chf00270
Entry
chf00270                    Pathway                                
Name
Cysteine and methionine metabolism - Chitinophaga pendula
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
chf00270  Cysteine and methionine metabolism
chf00270

Other DBs
GO: 0006534 0006555
Organism
Chitinophaga pendula [GN:chf]
Gene
KTO58_16140  serine O-acetyltransferase [KO:K00640] [EC:2.3.1.30]
KTO58_20825  serine acetyltransferase [KO:K00640] [EC:2.3.1.30]
KTO58_07360  PLP-dependent aspartate aminotransferase family protein [KO:K01760] [EC:4.4.1.13]
KTO58_17125  PLP-dependent aspartate aminotransferase family protein [KO:K01760] [EC:4.4.1.13]
KTO58_25370  cystathionine gamma-synthase [KO:K01760] [EC:4.4.1.13]
KTO58_08345  pyridoxal-phosphate dependent enzyme [KO:K01697] [EC:4.2.1.22]
KTO58_23065  metH; methionine synthase [KO:K00548] [EC:2.1.1.13]
KTO58_23060  homocysteine S-methyltransferase family protein [KO:K00548] [EC:2.1.1.13]
KTO58_02525  metE; 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase [KO:K00549] [EC:2.1.1.14]
KTO58_11680  metE; 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase [KO:K00549] [EC:2.1.1.14]
KTO58_08475  metK; methionine adenosyltransferase [KO:K00789] [EC:2.5.1.6]
KTO58_12620  GAF domain-containing protein [KO:K08968] [EC:1.8.4.14]
KTO58_16510  ahcY; adenosylhomocysteinase [KO:K01251] [EC:3.13.2.1]
KTO58_17460  pyridoxal-phosphate dependent enzyme [KO:K01505] [EC:3.5.99.7]
KTO58_00810  aspartate kinase [KO:K00928] [EC:2.7.2.4]
KTO58_06270  aspartate kinase [KO:K00928] [EC:2.7.2.4]
KTO58_15510  aspartate kinase [KO:K00928] [EC:2.7.2.4]
KTO58_06150  thrA; bifunctional aspartate kinase/homoserine dehydrogenase I [KO:K12524] [EC:2.7.2.4 1.1.1.3]
KTO58_25060  aspartate-semialdehyde dehydrogenase [KO:K00133] [EC:1.2.1.11]
KTO58_17130  homoserine dehydrogenase [KO:K00003] [EC:1.1.1.3]
KTO58_08755  metX; homoserine O-acetyltransferase [KO:K00641] [EC:2.3.1.31 2.3.1.46]
KTO58_14405  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase [KO:K01740] [EC:2.5.1.49]
KTO58_08765  O-succinylhomoserine sulfhydrylase [KO:K10764] [EC:2.5.1.-]
KTO58_17435  branched-chain amino acid transaminase [KO:K00826] [EC:2.6.1.42]
KTO58_18730  branched-chain amino acid aminotransferase [KO:K00826] [EC:2.6.1.42]
KTO58_03995  pyridoxal phosphate-dependent aminotransferase [KO:K00812] [EC:2.6.1.1]
KTO58_18510  pyridoxal phosphate-dependent aminotransferase [KO:K00812] [EC:2.6.1.1]
KTO58_24520  pyridoxal phosphate-dependent aminotransferase [KO:K00812] [EC:2.6.1.1]
KTO58_08705  sulfurtransferase [KO:K01011] [EC:2.8.1.1 2.8.1.2]
KTO58_18415  mdh; malate dehydrogenase [KO:K00024] [EC:1.1.1.37]
KTO58_09305  D-cysteine desulfhydrase family protein [KO:K17950] [EC:4.4.1.25]
KTO58_04065  L-serine ammonia-lyase [KO:K01752] [EC:4.3.1.17]
KTO58_16145  cysM; cysteine synthase CysM [KO:K12339] [EC:2.5.1.144]
KTO58_09060  serA; phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]
KTO58_21080  hydroxyacid dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]
KTO58_21690  serC; 3-phosphoserine/phosphohydroxythreonine transaminase [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
chf00010  Glycolysis / Gluconeogenesis
chf00250  Alanine, aspartate and glutamate metabolism
chf00260  Glycine, serine and threonine metabolism
chf00290  Valine, leucine and isoleucine biosynthesis
chf00430  Taurine and hypotaurine metabolism
chf00480  Glutathione metabolism
chf00620  Pyruvate metabolism
chf00640  Propanoate metabolism
chf00770  Pantothenate and CoA biosynthesis
chf00900  Terpenoid backbone biosynthesis
chf00920  Sulfur metabolism
KO pathway
ko00270   
LinkDB

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