KEGG PATHWAY: mhaa00270

PATHWAY: mhaa00270

Entry

mhaa00270                   Pathway

Name

Cysteine and methionine metabolism - Marivirga harenae

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

mhaa00270

Cysteine and methionine metabolism

Module

mhaa_M00035

Methionine degradation [PATH:mhaa00270]

Other DBs

GO:	0006534 0006555

Organism

Marivirga harenae [GN:mhaa]

Gene

Q3Y49_17460

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

Q3Y49_11960

cystathionine gamma-synthase [KO:K01760] [EC:4.4.1.13]

Q3Y49_12775

cystathionine beta-synthase [KO:K01697] [EC:4.2.1.22]

Q3Y49_12310

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

Q3Y49_07270

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

Q3Y49_01285

phosphotransferase [KO:K00899] [EC:2.7.1.100]

Q3Y49_17175

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

Q3Y49_10815

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

Q3Y49_14685

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

Q3Y49_02195

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

Q3Y49_08120

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

Q3Y49_05400

pyridoxal-phosphate dependent enzyme [KO:K01505] [EC:3.5.99.7]

Q3Y49_04465

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

Q3Y49_08300

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

Q3Y49_02695

thrA; bifunctional aspartate kinase/homoserine dehydrogenase I [KO:K12524] [EC:2.7.2.4 1.1.1.3]

Q3Y49_05380

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

Q3Y49_17890

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

Q3Y49_17885

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

Q3Y49_17880

O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase [KO:K01740] [EC:2.5.1.49]

Q3Y49_02415

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme [KO:K10764] [EC:2.5.1.-]

Q3Y49_12355

aminotransferase class IV [KO:K00826] [EC:2.6.1.42]

Q3Y49_15340

aminotransferase class IV [KO:K00826] [EC:2.6.1.42]

Q3Y49_16970

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

Q3Y49_01965

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

Q3Y49_07665

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

Q3Y49_01110

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

Q3Y49_16700

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

Q3Y49_12350

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

Q3Y49_07060

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

Q3Y49_17475

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

Q3Y49_13145

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

Q3Y49_10610

NAD(P)-dependent oxidoreductase [KO:K00058] [EC:1.1.1.95 1.1.1.399]

Q3Y49_11785

aminotransferase class V-fold PLP-dependent enzyme [KO:K00831] [EC:2.6.1.52]

Q3Y49_17795

aminotransferase class V-fold PLP-dependent enzyme [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