KEGG PATHWAY: bsul00270

PATHWAY: bsul00270

Entry

bsul00270                   Pathway

Name

Cysteine and methionine metabolism - Bacillus subtilis subsp. subtilis JH642

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

bsul00270

Cysteine and methionine metabolism

Module

bsul_M00017

Methionine biosynthesis, aspartate => homoserine => methionine [PATH:bsul00270]

bsul_M00021

Cysteine biosynthesis, serine => cysteine [PATH:bsul00270]

bsul_M00034

Methionine salvage pathway [PATH:bsul00270]

bsul_M00609

Cysteine biosynthesis, methionine => cysteine [PATH:bsul00270]

Other DBs

GO:	0006534 0006555

Organism

Bacillus subtilis subsp. subtilis JH642 [GN:bsul]

Gene

BSUA_00121

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

BSUA_03188

ytkP; cysteine synthase-like protein [KO:K01738] [EC:2.5.1.47]

BSUA_00086

cysK; cysteine synthase [KO:K01738] [EC:2.5.1.47]

BSUA_02907

mccB; cystathionine beta-lyase [KO:K17217] [EC:4.4.1.1 4.4.1.2]

BSUA_01291

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

BSUA_03362

patB; C-S lyase [KO:K14155] [EC:4.4.1.13]

BSUA_02908

mccA; cystathionine beta-synthase [KO:K17216] [EC:2.5.1.134]

BSUA_00289

ybgG; homocysteine methyltransferase [KO:K00547] [EC:2.1.1.10]

BSUA_01198

yitJ; bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase [KO:K24042] [EC:2.1.1.13 1.5.1.54]

BSUA_01436

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

BSUA_03245

metK; S-adenosylmethionine synthetase [KO:K00789] [EC:2.5.1.6]

BSUA_03089

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

BSUA_03985

speE; spermidine synthase [KO:K00797] [EC:2.5.1.16]

BSUA_02909

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

BSUA_01476

mtnK; methylthioribose kinase [KO:K00899] [EC:2.7.1.100]

BSUA_01667

ylmD; hypothetical protein [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

BSUA_01475

mtnA; methylthioribose-1-phosphate isomerase [KO:K08963] [EC:5.3.1.23]

BSUA_01481

mtnB; methylthioribulose-1-phosphate dehydratase [KO:K08964] [EC:4.2.1.109]

BSUA_01479

mtnW; 2,3-diketo-5-methylthiopentyl-1-phosphate enolase [KO:K08965] [EC:5.3.2.5]

BSUA_01480

mtnX; 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase [KO:K08966] [EC:3.1.3.87]

BSUA_01482

mtnD; acireductone dioxygenase [KO:K08967] [EC:1.13.11.53 1.13.11.54]

BSUA_01478

mtnE; transaminase [KO:K08969] [EC:2.6.1.117]

BSUA_03154

ytsP; hypothetical protein [KO:K08968] [EC:1.8.4.14]

BSUA_00673

ydiO; DNA-methyltransferase [KO:K00558] [EC:2.1.1.37]

BSUA_00674

ydiP; DNA-methyltransferase [KO:K00558] [EC:2.1.1.37]

BSUA_02182

mtbP; SP-beta prophage DNA (cytosine-5-)-methyltransferase [KO:K00558] [EC:2.1.1.37]

BSUA_02910

yrrT; AdoMet-dependent methyltransferase [KO:K17462] [EC:2.1.1.-]

BSUA_03257

luxS; S-ribosylhomocysteinase [KO:K07173] [EC:4.4.1.21]

BSUA_00430

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

BSUA_01808

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

BSUA_03035

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

BSUA_01807

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

BSUA_03444

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

BSUA_02356

metA; homoserine O-succinyltransferase [KO:K00651] [EC:2.3.1.46 2.3.1.31]

BSUA_01290

metI; cystathionine gamma-synthase [KO:K01739] [EC:2.5.1.48]

BSUA_00287

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

BSUA_04094

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

BSUA_03328

cdoA; cysteine dioxygenase [KO:K00456] [EC:1.13.11.20]

BSUA_02404

aspB; aspartate aminotransferase [KO:K00812] [EC:2.6.1.1]

BSUA_01052

yhdR; aspartate aminotransferase [KO:K11358] [EC:2.6.1.1]

BSUA_00354

ldh; L-lactate dehydrogenase [KO:K00016] [EC:1.1.1.27]

BSUA_03671

racX; amino acid racemase [KO:K25316] [EC:5.1.1.10]

BSUA_03100

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

BSUA_01716

sdaAB; L-serine dehydratase subunit beta [KO:K01752] [EC:4.3.1.17]

BSUA_01717

sdaAA; L-serine dehydratase subunit alpha [KO:K01752] [EC:4.3.1.17]

BSUA_01995

yoaD; 2-hydroxyacid dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]

BSUA_02476

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

BSUA_01099

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

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