KEGG   PATHWAY: aqb00270
Entry
aqb00270                    Pathway                                
Name
Cysteine and methionine metabolism - Aquimarina sp. BL5
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
aqb00270  Cysteine and methionine metabolism
aqb00270

Module
aqb_M00035  Methionine degradation [PATH:aqb00270]
aqb_M00338  Cysteine biosynthesis, homocysteine + serine => cysteine [PATH:aqb00270]
Other DBs
GO: 0006534 0006555
Organism
Aquimarina sp. BL5 [GN:aqb]
Gene
D1818_01565  serine acetyltransferase [KO:K00640] [EC:2.3.1.30]
D1818_02925  serine acetyltransferase [KO:K00640] [EC:2.3.1.30]
D1818_13380  cystathionine gamma-synthase [KO:K01758] [EC:4.4.1.1]
D1818_24545  PLP-dependent transferase [KO:K01760] [EC:4.4.1.13]
D1818_03970  cysteine synthase family protein [KO:K01697] [EC:4.2.1.22]
D1818_08545  pyridoxal-phosphate dependent enzyme [KO:K01697] [EC:4.2.1.22]
D1818_10395  methionine synthase [KO:K00548] [EC:2.1.1.13]
D1818_10400  5-methyltetrahydrofolate--homocysteine methyltransferase [KO:K00548] [EC:2.1.1.13]
D1818_10485  methionine adenosyltransferase [KO:K00789] [EC:2.5.1.6]
D1818_05710  methyltransferase domain-containing protein [KO:K00797] [EC:2.5.1.16]
D1818_04065  cystathionine gamma-synthase family protein [KO:K01761] [EC:4.4.1.11]
D1818_17395  GAF domain-containing protein [KO:K08968] [EC:1.8.4.14]
D1818_05490  DNA cytosine methyltransferase [KO:K00558] [EC:2.1.1.37]
D1818_05535  DNA cytosine methyltransferase [KO:K00558] [EC:2.1.1.37]
D1818_11085  dcm; DNA (cytosine-5-)-methyltransferase [KO:K00558] [EC:2.1.1.37]
D1818_11130  DNA cytosine methyltransferase [KO:K00558] [EC:2.1.1.37]
D1818_16000  adenosylhomocysteinase [KO:K01251] [EC:3.13.2.1]
D1818_18700  1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase [KO:K01505] [EC:3.5.99.7]
D1818_12700  aspartate kinase [KO:K00928] [EC:2.7.2.4]
D1818_23220  aspartate kinase [KO:K00928] [EC:2.7.2.4]
D1818_01365  bifunctional aspartate kinase/homoserine dehydrogenase I [KO:K12524] [EC:2.7.2.4 1.1.1.3]
D1818_15245  aspartate-semialdehyde dehydrogenase [KO:K00133] [EC:1.2.1.11]
D1818_10480  O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase [KO:K01740] [EC:2.5.1.49]
D1818_10465  aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [KO:K10764] [EC:2.5.1.-]
D1818_21340  branched-chain amino acid aminotransferase [KO:K00826] [EC:2.6.1.42]
D1818_00275  aminotransferase class IV [KO:K00826] [EC:2.6.1.42]
D1818_18235  branched-chain amino acid aminotransferase [KO:K00826] [EC:2.6.1.42]
D1818_09385  pyridoxal phosphate-dependent aminotransferase [KO:K00812] [EC:2.6.1.1]
D1818_20710  pyridoxal phosphate-dependent aminotransferase [KO:K00812] [EC:2.6.1.1]
D1818_14000  sulfurtransferase [KO:K01011] [EC:2.8.1.1 2.8.1.2]
D1818_08855  mdh; malate dehydrogenase [KO:K00024] [EC:1.1.1.37]
D1818_23880  L-serine ammonia-lyase [KO:K01752] [EC:4.3.1.17]
D1818_01560  cysM; cysteine synthase CysM [KO:K12339] [EC:2.5.1.144]
D1818_03655  3-phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]
D1818_12625  hydroxyacid dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]
D1818_03650  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
aqb00010  Glycolysis / Gluconeogenesis
aqb00250  Alanine, aspartate and glutamate metabolism
aqb00260  Glycine, serine and threonine metabolism
aqb00290  Valine, leucine and isoleucine biosynthesis
aqb00430  Taurine and hypotaurine metabolism
aqb00480  Glutathione metabolism
aqb00620  Pyruvate metabolism
aqb00640  Propanoate metabolism
aqb00770  Pantothenate and CoA biosynthesis
aqb00900  Terpenoid backbone biosynthesis
aqb00920  Sulfur metabolism
KO pathway
ko00270   
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