KEGG   PATHWAY: bbrx00270
Entry
bbrx00270                   Pathway                                
Name
Cysteine and methionine metabolism - Brettanomyces bruxellensis
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
bbrx00270  Cysteine and methionine metabolism
bbrx00270

Module
bbrx_M00017  Methionine biosynthesis, aspartate => homoserine => methionine [PATH:bbrx00270]
bbrx_M00034  Methionine salvage pathway [PATH:bbrx00270]
Other DBs
GO: 0006534 0006555
Organism
Brettanomyces bruxellensis [GN:bbrx]
Gene
BRETT_003357  uncharacterized protein [KO:K01738] [EC:2.5.1.47]
BRETT_004777  uncharacterized protein [KO:K01738] [EC:2.5.1.47]
BRETT_004417  MET17; Homocysteine synthase [KO:K17069] [EC:2.5.1.49 2.5.1.47]
BRETT_004186  uncharacterized protein [KO:K01760] [EC:4.4.1.13]
BRETT_002002  uncharacterized protein [KO:K00547] [EC:2.1.1.10]
BRETT_001380  MET6; methionine-synthesizing 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase [KO:K00549] [EC:2.1.1.14]
BRETT_001354  SAM1; methionine adenosyltransferase sam1 [KO:K00789] [EC:2.5.1.6]
BRETT_001242  uncharacterized protein [KO:K01611] [EC:4.1.1.50]
BRETT_001090  SPE3; putrescine aminopropyltransferase [KO:K00797] [EC:2.5.1.16]
BRETT_003792  uncharacterized protein [KO:K00802] [EC:2.5.1.22]
BRETT_001157  MEU1; S-methyl-5-thioadenosine phosphorylase [KO:K00772] [EC:2.4.2.28]
BRETT_004139  uncharacterized protein [KO:K08963] [EC:5.3.1.23]
BRETT_004982  MDE1; Methylthioribulose-1-phosphate dehydratase [KO:K08964] [EC:4.2.1.109]
BRETT_004341  uncharacterized protein [KO:K09880] [EC:3.1.3.77]
BRETT_000316  uncharacterized protein [KO:K08967] [EC:1.13.11.53 1.13.11.54]
BRETT_001037  uncharacterized protein [KO:K00838] [EC:2.6.1.57 2.6.1.39 2.6.1.27 2.6.1.5]
BRETT_003919  uncharacterized protein [KO:K00838] [EC:2.6.1.57 2.6.1.39 2.6.1.27 2.6.1.5]
BRETT_004274  uncharacterized protein [KO:K08968] [EC:1.8.4.14]
BRETT_004284  SAH1; S-adenosyl-L-homocysteine hydrolase [KO:K01251] [EC:3.13.2.1]
BRETT_003472  uncharacterized protein [KO:K00928] [EC:2.7.2.4]
BRETT_003663  HOM2; aspartate-semialdehyde dehydrogenase [KO:K00133] [EC:1.2.1.11]
BRETT_000422  HOM6; Homoserine dehydrogenase [KO:K00003] [EC:1.1.1.3]
BRETT_001765  uncharacterized protein [KO:K00641] [EC:2.3.1.31 2.3.1.46]
BRETT_005207  uncharacterized protein [KO:K01739] [EC:2.5.1.48]
BRETT_004300  BAT1; Mitochondrial branched-chain amino acid (BCAA) aminotransferase [KO:K00826] [EC:2.6.1.42]
BRETT_004126  uncharacterized protein [KO:K11204] [EC:6.3.2.2]
BRETT_003059  uncharacterized protein [KO:K21456] [EC:6.3.2.3]
BRETT_001995  uncharacterized protein [KO:K00456] [EC:1.13.11.20]
BRETT_001787  uncharacterized protein [KO:K14454] [EC:2.6.1.1]
BRETT_003118  uncharacterized protein [KO:K14455] [EC:2.6.1.1]
BRETT_002579  uncharacterized protein [KO:K01011] [EC:2.8.1.1 2.8.1.2]
BRETT_005005  MDH1; Malate dehydrogenase, cytoplasmic [KO:K00026] [EC:1.1.1.37]
BRETT_000987  uncharacterized protein [KO:K00026] [EC:1.1.1.37]
BRETT_003953  uncharacterized protein [KO:K00026] [EC:1.1.1.37]
BRETT_003192  SER33; D-3-phosphoglycerate dehydrogenase 2 [KO:K00058] [EC:1.1.1.95 1.1.1.399]
BRETT_002496  uncharacterized protein [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
bbrx00010  Glycolysis / Gluconeogenesis
bbrx00250  Alanine, aspartate and glutamate metabolism
bbrx00260  Glycine, serine and threonine metabolism
bbrx00290  Valine, leucine and isoleucine biosynthesis
bbrx00430  Taurine and hypotaurine metabolism
bbrx00480  Glutathione metabolism
bbrx00620  Pyruvate metabolism
bbrx00640  Propanoate metabolism
bbrx00770  Pantothenate and CoA biosynthesis
bbrx00900  Terpenoid backbone biosynthesis
bbrx00920  Sulfur metabolism
KO pathway
ko00270   
LinkDB

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