KEGG PATHWAY: pms00270

PATHWAY: pms00270

Entry

pms00270                    Pathway

Name

Cysteine and methionine metabolism - Paenibacillus mucilaginosus KNP414

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

pms00270

Cysteine and methionine metabolism

Module

pms_M00017

Methionine biosynthesis, aspartate => homoserine => methionine [PATH:pms00270]

pms_M00021

Cysteine biosynthesis, serine => cysteine [PATH:pms00270]

pms_M00034

Methionine salvage pathway [PATH:pms00270]

Other DBs

GO:	0006534 0006555

Organism

Paenibacillus mucilaginosus KNP414 [GN:pms]

Gene

KNP414_04498

cysE; CysE [KO:K00640] [EC:2.3.1.30]

KNP414_07545

cysE3; CysE3 [KO:K00640] [EC:2.3.1.30]

KNP414_05064

cysE2; CysE2 [KO:K00640] [EC:2.3.1.30]

KNP414_06803

ytkP; YtkP [KO:K01738] [EC:2.5.1.47]

KNP414_07570

cysK2; CysK2 [KO:K01738] [EC:2.5.1.47]

KNP414_05594

cysK; CysK [KO:K01738] [EC:2.5.1.47]

KNP414_06190

aminotransferase class I and II [KO:K14155] [EC:4.4.1.13]

KNP414_02921

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

KNP414_05916

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

KNP414_04334

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

KNP414_04838

metE; MetE [KO:K00549] [EC:2.1.1.14]

KNP414_00091

metK; MetK [KO:K00789] [EC:2.5.1.6]

KNP414_05363

speD; SpeD [KO:K01611] [EC:4.1.1.50]

KNP414_06474

speH; SpeH [KO:K01611] [EC:4.1.1.50]

KNP414_07659

speE; SpeE [KO:K00797] [EC:2.5.1.16]

KNP414_02286

Spermine synthase [KO:K00797] [EC:2.5.1.16]

KNP414_03913

Adenosylhomocysteine nucleosidase [KO:K01243] [EC:3.2.2.9]

KNP414_01098

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

KNP414_04054

protein of unknown function DUF152 [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

KNP414_00825

amidohydrolase [KO:K12960] [EC:3.5.4.31 3.5.4.28]

KNP414_01445

hypothetical protein [KO:K12960] [EC:3.5.4.31 3.5.4.28]

KNP414_02831

cytosine deaminase-related metal-dependent hydrolase [KO:K12960] [EC:3.5.4.31 3.5.4.28]

KNP414_01076

N-ethylammeline chlorohydrolase [KO:K12960] [EC:3.5.4.31 3.5.4.28]

KNP414_01097

mtnA1; MtnA1 [KO:K08963] [EC:5.3.1.23]

KNP414_04028

mtnB; MtnB [KO:K08964] [EC:4.2.1.109]

KNP414_04026

mtnW; MtnW [KO:K08965] [EC:5.3.2.5]

KNP414_04027

mtnX; MtnX [KO:K08966] [EC:3.1.3.87]

KNP414_02920

mtnD; MtnD [KO:K08967] [EC:1.13.11.53 1.13.11.54]

KNP414_04020

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

KNP414_03260

ytsP; YtsP [KO:K08968] [EC:1.8.4.14]

KNP414_01203

C-5 cytosine-specific DNA methylase [KO:K00558] [EC:2.1.1.37]

KNP414_02488

probable transcriptional regulator [KO:K17462] [EC:2.1.1.-]

KNP414_04076

ahcY; AhcY [KO:K01251] [EC:3.13.2.1]

KNP414_02658

lysC; LysC [KO:K00928] [EC:2.7.2.4]

KNP414_05757

dapG; DapG [KO:K00928] [EC:2.7.2.4]

KNP414_06141

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

KNP414_05758

asd; Asd [KO:K00133] [EC:1.2.1.11]

KNP414_06428

hom; Hom [KO:K00003] [EC:1.1.1.3]

KNP414_06427

homoserine kinase [KO:K00872] [EC:2.7.1.39]

KNP414_06768

metA; MetA [KO:K00651] [EC:2.3.1.46 2.3.1.31]

KNP414_01154

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

KNP414_06767

metB; MetB [KO:K01739] [EC:2.5.1.48]

KNP414_02498

cysD; CysD [KO:K01740] [EC:2.5.1.49]

KNP414_02496

ilvK; IlvK [KO:K00826] [EC:2.6.1.42]

KNP414_06634

hypothetical protein [KO:K00456] [EC:1.13.11.20]

KNP414_07672

Rhodanese domain protein [KO:K01011] [EC:2.8.1.1 2.8.1.2]

KNP414_04970

Rhodanese-related sulfurtransferase-like protein [KO:K01011] [EC:2.8.1.1 2.8.1.2]

KNP414_03680

ldh; Ldh [KO:K00016] [EC:1.1.1.27]

KNP414_05253

ldh2; Ldh2 [KO:K00016] [EC:1.1.1.27]

KNP414_02511

ygeA; YgeA [KO:K25316] [EC:5.1.1.10]

KNP414_01283

mdh; Mdh [KO:K00024] [EC:1.1.1.37]

KNP414_05049

L-serine dehydratase, iron-sulfur-dependent, alpha subunit [KO:K01752] [EC:4.3.1.17]

KNP414_05050

L-serine dehydratase, iron-sulfur-dependent, beta subunit [KO:K01752] [EC:4.3.1.17]

KNP414_02744

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

KNP414_06705

serC; SerC [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

C01102

O-Phospho-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