KEGG PATHWAY: shua00270

PATHWAY: shua00270

Entry

shua00270                   Pathway

Name

Cysteine and methionine metabolism - Shouchella hunanensis

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

shua00270

Cysteine and methionine metabolism

Module

shua_M00017

Methionine biosynthesis, aspartate => homoserine => methionine [PATH:shua00270]

shua_M00021

Cysteine biosynthesis, serine => cysteine [PATH:shua00270]

shua_M00034

Methionine salvage pathway [PATH:shua00270]

Other DBs

GO:	0006534 0006555

Organism

Shouchella hunanensis [GN:shua]

Gene

PQ477_08330

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

PQ477_01930

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

PQ477_08155

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

PQ477_17365

bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase [KO:K17217] [EC:4.4.1.1 4.4.1.2]

PQ477_02070

pyridoxal phosphate-dependent aminotransferase [KO:K14155] [EC:4.4.1.13]

PQ477_17360

cysteine synthase family protein [KO:K17216] [EC:2.5.1.134]

PQ477_07390

mmuM; homocysteine S-methyltransferase [KO:K00547] [EC:2.1.1.10]

PQ477_19135

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

PQ477_19140

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

PQ477_14860

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

PQ477_02020

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

PQ477_01540

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

PQ477_06430

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

PQ477_15565

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

PQ477_11635

mtnK; S-methyl-5-thioribose kinase [KO:K00899] [EC:2.7.1.100]

PQ477_20540

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

PQ477_10040

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

PQ477_11710

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

PQ477_18860

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

PQ477_11640

mtnA; S-methyl-5-thioribose-1-phosphate isomerase [KO:K08963] [EC:5.3.1.23]

PQ477_11620

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

PQ477_11630

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

PQ477_16795

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

PQ477_11625

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

PQ477_11615

AraC family ligand binding domain-containing protein [KO:K08967] [EC:1.13.11.53 1.13.11.54]

PQ477_11610

pyridoxal phosphate-dependent aminotransferase [KO:K08969] [EC:2.6.1.117]

PQ477_01790

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

PQ477_08880

DNA cytosine methyltransferase [KO:K00558] [EC:2.1.1.37]

PQ477_08890

dcm; DNA (cytosine-5-)-methyltransferase [KO:K00558] [EC:2.1.1.37]

PQ477_02245

S-ribosylhomocysteine lyase [KO:K07173] [EC:4.4.1.21]

PQ477_16715

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

PQ477_19880

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

PQ477_19885

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

PQ477_07705

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

PQ477_15445

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

PQ477_19570

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

PQ477_07695

cystathionine gamma-synthase family protein [KO:K01739] [EC:2.5.1.48]

PQ477_19145

methionine biosynthesis PLP-dependent protein [KO:K01739] [EC:2.5.1.48]

PQ477_17280

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

PQ477_07115

cysteine dioxygenase family protein [KO:K00456] [EC:1.13.11.20]

PQ477_03985

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

PQ477_18490

aspartate/glutamate racemase family protein [KO:K25316] [EC:5.1.1.10]

PQ477_01590

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

PQ477_20345

sdaAA; L-serine ammonia-lyase, iron-sulfur-dependent, subunit alpha [KO:K01752] [EC:4.3.1.17]

PQ477_20350

sdaAB; L-serine ammonia-lyase, iron-sulfur-dependent subunit beta [KO:K01752] [EC:4.3.1.17]

PQ477_06660

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

PQ477_13830

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

PQ477_19245

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

PQ477_15205

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