KEGG PATHWAY: apes00270

PATHWAY: apes00270

Entry

apes00270                   Pathway

Name

Cysteine and methionine metabolism - Achromobacter pestifer

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

apes00270

Cysteine and methionine metabolism

Other DBs

GO:	0006534 0006555

Organism

Achromobacter pestifer [GN:apes]

Gene

FOC84_23495

serine acetyltransferase [KO:K00640] [EC:2.3.1.30]

FOC84_12185

metC; cystathionine beta-lyase [KO:K01760] [EC:4.4.1.13]

FOC84_16415

metC; cystathionine beta-lyase [KO:K01760] [EC:4.4.1.13]

FOC84_30585

metC; cystathionine beta-lyase [KO:K01760] [EC:4.4.1.13]

FOC84_09975

metH; methionine synthase [KO:K00548] [EC:2.1.1.13]

FOC84_33015

methionine synthase [KO:K00549] [EC:2.1.1.14]

FOC84_03205

metE; 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase [KO:K00549] [EC:2.1.1.14]

FOC84_13995

methionine adenosyltransferase [KO:K00789] [EC:2.5.1.6]

FOC84_23925

speD; adenosylmethionine decarboxylase [KO:K01611] [EC:4.1.1.50]

FOC84_11525

fused MFS/spermidine synthase [KO:K00797] [EC:2.5.1.16]

FOC84_23900

polyamine aminopropyltransferase [KO:K00797] [EC:2.5.1.16]

FOC84_01470

fused MFS/spermidine synthase [KO:K00797] [EC:2.5.1.16]

FOC84_29300

fused MFS/spermidine synthase [KO:K00797] [EC:2.5.1.16]

FOC84_17195

5'-methylthioadenosine/adenosylhomocysteine nucleosidase [KO:K01243] [EC:3.2.2.9]

FOC84_04275

pgeF; peptidoglycan editing factor PgeF [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

FOC84_22570

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [KO:K00832] [EC:2.6.1.57]

FOC84_25750

aspartate/tyrosine/aromatic aminotransferase [KO:K00832] [EC:2.6.1.57]

FOC84_24400

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [KO:K01761] [EC:4.4.1.11]

FOC84_27220

cystathionine gamma-synthase family protein [KO:K01761] [EC:4.4.1.11]

FOC84_13605

GAF domain-containing protein [KO:K08968] [EC:1.8.4.14]

FOC84_14050

adenosylhomocysteinase [KO:K01251] [EC:3.13.2.1]

FOC84_04380

1-aminocyclopropane-1-carboxylate deaminase [KO:K01505] [EC:3.5.99.7]

FOC84_23140

aspartate kinase [KO:K00928] [EC:2.7.2.4]

FOC84_01730

asd; aspartate-semialdehyde dehydrogenase [KO:K00133] [EC:1.2.1.11]

FOC84_03065

homoserine dehydrogenase [KO:K00003] [EC:1.1.1.3]

FOC84_10120

homoserine O-acetyltransferase [KO:K00641] [EC:2.3.1.31 2.3.1.46]

FOC84_05225

alpha/beta fold hydrolase [KO:K00641] [EC:2.3.1.31 2.3.1.46]

FOC84_30840

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [KO:K01740] [EC:2.5.1.49]

FOC84_02785

cystathionine gamma-synthase family protein [KO:K01740] [EC:2.5.1.49]

FOC84_05050

branched-chain amino acid aminotransferase [KO:K00826] [EC:2.6.1.42]

FOC84_07340

branched-chain amino acid transaminase [KO:K00826] [EC:2.6.1.42]

FOC84_10175

glutamate--cysteine ligase [KO:K01919] [EC:6.3.2.2]

FOC84_01585

gshB; glutathione synthase [KO:K01920] [EC:6.3.2.3]

FOC84_18325

pyridoxal phosphate-dependent aminotransferase [KO:K00812] [EC:2.6.1.1]

FOC84_03500

sulfurtransferase [KO:K01011] [EC:2.8.1.1 2.8.1.2]

FOC84_14405

Ldh family oxidoreductase [KO:K00016] [EC:1.1.1.27]

FOC84_03915

bifunctional aspartate transaminase/aspartate 4-decarboxylase [KO:K09758] [EC:4.1.1.12]

FOC84_10145

hydroxyacid dehydrogenase [KO:K16843] [EC:1.1.1.310]

FOC84_04460

malate dehydrogenase [KO:K00024] [EC:1.1.1.37]

FOC84_10150

Ldh family oxidoreductase [KO:K16844] [EC:1.1.1.338]

FOC84_10130

UxaA family hydrolase [KO:K16845] [EC:4.4.1.24]

FOC84_10135

UxaA family hydrolase [KO:K16846] [EC:4.4.1.24]

FOC84_03515

L-serine ammonia-lyase [KO:K01752] [EC:4.3.1.17]

FOC84_08920

pyridoxal-phosphate dependent enzyme [KO:K17989] [EC:4.3.1.17 4.3.1.19]

FOC84_03960

cysM; cysteine synthase CysM [KO:K12339] [EC:2.5.1.144]

FOC84_10065

serA; phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]

FOC84_24875

hydroxyacid dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]

FOC84_28990

3-phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]

FOC84_07245

D-2-hydroxyacid dehydrogenase family protein [KO:K00058] [EC:1.1.1.95 1.1.1.399]

FOC84_16965

serC; 3-phosphoserine/phosphohydroxythreonine transaminase [KO:K00831] [EC:2.6.1.52]

FOC84_04025

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

PMID:15102328

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

PMID:14551435

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

PMID:12022921

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

PMID:12670965

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

PMID:17169919

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

PMID:17030798

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

PMID:18625006

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

PMID:18391471

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

PMID:10613873

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

PMID:12644499

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

PMID:18520135

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

PMID:19270684

Authors