KEGG PATHWAY: otm00270

PATHWAY: otm00270

Entry

otm00270                    Pathway

Name

Cysteine and methionine metabolism - Octadecabacter temperatus

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

otm00270

Cysteine and methionine metabolism

Module

otm_M00021

Cysteine biosynthesis, serine => cysteine [PATH:otm00270]

Other DBs

GO:	0006534 0006555

Organism

Octadecabacter temperatus [GN:otm]

Gene

OSB_19390

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

OSB_12970

mccA; O-acetylserine dependent cystathionine beta-synthase [KO:K01738] [EC:2.5.1.47]

OSB_01970

patB; Cystathionine beta-lyase PatB [KO:K14155] [EC:4.4.1.13]

OSB_17760

yitJ; Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase [KO:K00548] [EC:2.1.1.13]

OSB_15390

acsE; 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase [KO:K00548] [EC:2.1.1.13]

OSB_24540

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

OSB_07670

mtnP; S-methyl-5'-thioadenosine phosphorylase [KO:K00772] [EC:2.4.2.28]

OSB_06830

yfiH; Laccase domain protein YfiH [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

OSB_03240

mdeA_1; Methionine gamma-lyase [KO:K01761] [EC:4.4.1.11]

OSB_30310

msrC; Free methionine-R-sulfoxide reductase [KO:K08968] [EC:1.8.4.14]

OSB_32360

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

OSB_07600

ask; Aspartokinase [KO:K00928] [EC:2.7.2.4]

OSB_00990

asd2; Aspartate-semialdehyde dehydrogenase 2 [KO:K00133] [EC:1.2.1.11]

OSB_22570

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

OSB_14050

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

OSB_10550

mdeA_2; Methionine gamma-lyase [KO:K01740] [EC:2.5.1.49]

OSB_09590

metZ; O-succinylhomoserine sulfhydrylase [KO:K10764] [EC:2.5.1.-]

OSB_22810

ilvE_1; Branched-chain-amino-acid aminotransferase [KO:K00826] [EC:2.6.1.42]

OSB_31250

ilvE_2; Branched-chain-amino-acid aminotransferase [KO:K00826] [EC:2.6.1.42]

OSB_29010

gshA; Glutamate--cysteine ligase GshA [KO:K01919] [EC:6.3.2.2]

OSB_05200

gshB; Glutathione synthetase [KO:K01920] [EC:6.3.2.3]

OSB_09840

Aspartate aminotransferase [KO:K00812] [EC:2.6.1.1]

OSB_01530

tyrB; Aromatic-amino-acid aminotransferase [KO:K00813] [EC:2.6.1.1]

OSB_01540

sseA; 3-mercaptopyruvate sulfurtransferase [KO:K01011] [EC:2.8.1.1 2.8.1.2]

OSB_04730

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

OSB_22100

comC; (2R)-3-sulfolactate dehydrogenase (NADP(+)) [KO:K16844] [EC:1.1.1.338]

OSB_10370

tdcG; L-serine dehydratase TdcG [KO:K01752] [EC:4.3.1.17]

OSB_00290

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

OSB_00300

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

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