KEGG PATHWAY: sxt00270

PATHWAY: sxt00270

Entry

sxt00270                    Pathway

Name

Cysteine and methionine metabolism - Streptomyces xanthophaeus

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

sxt00270

Cysteine and methionine metabolism

Module

sxt_M00035

Methionine degradation [PATH:sxt00270]

sxt_M00338

Cysteine biosynthesis, homocysteine + serine => cysteine [PATH:sxt00270]

Other DBs

GO:	0006534 0006555

Organism

Streptomyces xanthophaeus [GN:sxt]

Gene

KPP03845_106533

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

KPP03845_101190

sbnA_1; putative siderophore biosynthesis protein SbnA [KO:K01738] [EC:2.5.1.47]

KPP03845_103904

metB_1; Cystathionine gamma-synthase [KO:K01758] [EC:4.4.1.1]

KPP03845_103181

cbs; Putative cystathionine beta-synthase [KO:K01697] [EC:4.2.1.22]

KPP03845_105632

mmuM_2; Homocysteine S-methyltransferase [KO:K00547] [EC:2.1.1.10]

KPP03845_300059

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

KPP03845_101889

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

KPP03845_106594

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

KPP03845_300061

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

KPP03845_101550

metK_1; S-adenosylmethionine synthase [KO:K00789] [EC:2.5.1.6]

KPP03845_101712

metK_2; S-adenosylmethionine synthase [KO:K00789] [EC:2.5.1.6]

KPP03845_103688

speE_3; Polyamine aminopropyltransferase [KO:K00797] [EC:2.5.1.16]

KPP03845_101547

mtnP_1; S-methyl-5'-thioadenosine phosphorylase [KO:K00772] [EC:2.4.2.28]

KPP03845_103282

mtnP_2; S-methyl-5'-thioadenosine phosphorylase [KO:K00772] [EC:2.4.2.28]

KPP03845_102323

Polyphenol oxidase [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

KPP03845_101549

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

KPP03845_101548

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

KPP03845_101543

mtnC; Enolase-phosphatase E1 [KO:K09880] [EC:3.1.3.77]

KPP03845_101544

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

KPP03845_106166

bacF; Transaminase BacF [KO:K08969] [EC:2.6.1.117]

KPP03845_105771

aplIM; Modification methylase AplI [KO:K00558] [EC:2.1.1.37]

KPP03845_106019

hypothetical protein [KO:K00558] [EC:2.1.1.37]

KPP03845_300057

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

KPP03845_102881

ahcY_1; Adenosylhomocysteinase [KO:K01251] [EC:3.13.2.1]

KPP03845_103133

ahcY_2; Adenosylhomocysteinase [KO:K01251] [EC:3.13.2.1]

KPP03845_105019

dcyD; D-cysteine desulfhydrase [KO:K01505] [EC:3.5.99.7]

KPP03845_103657

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

KPP03845_102814

asd_1; Aspartate-semialdehyde dehydrogenase [KO:K00133] [EC:1.2.1.11]

KPP03845_103656

asd_2; Aspartate-semialdehyde dehydrogenase [KO:K00133] [EC:1.2.1.11]

KPP03845_103341

hom_1; Homoserine dehydrogenase [KO:K00003] [EC:1.1.1.3]

KPP03845_105091

hom_2; Homoserine dehydrogenase [KO:K00003] [EC:1.1.1.3]

KPP03845_107060

metXA; Homoserine O-acetyltransferase [KO:K00641] [EC:2.3.1.31 2.3.1.46]

KPP03845_104716

metB_2; Cystathionine gamma-synthase [KO:K01739] [EC:2.5.1.48]

KPP03845_107061

mdeA; L-methionine gamma-lyase [KO:K01740] [EC:2.5.1.49]

KPP03845_101784

dat_1; D-alanine aminotransferase [KO:K00826] [EC:2.6.1.42]

KPP03845_105266

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

KPP03845_106342

egtA; Glutamate--cysteine ligase EgtA [KO:K01919] [EC:6.3.2.2]

KPP03845_104471

aspB; Asparagine--oxo-acid transaminase [KO:K00812] [EC:2.6.1.1]

KPP03845_105957

aspC_1; Aspartate aminotransferase [KO:K00813] [EC:2.6.1.1]

KPP03845_104125

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

KPP03845_105057

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

KPP03845_105579

sseB; Putative thiosulfate sulfurtransferase SseB [KO:K01011] [EC:2.8.1.1 2.8.1.2]

KPP03845_104612

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

KPP03845_105201

sdaA; L-serine dehydratase 1 [KO:K01752] [EC:4.3.1.17]

KPP03845_101366

cysM_1; Cysteine synthase B [KO:K12339] [EC:2.5.1.144]

KPP03845_102816

serA_1; D-3-phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]

KPP03845_105247

serA_2; D-3-phosphoglycerate dehydrogenase [KO:K00058] [EC:1.1.1.95 1.1.1.399]

KPP03845_104289

serC; Phosphoserine aminotransferase [KO:K00831] [EC:2.6.1.52]

KPP03845_100605

cysK2; S-sulfocysteine synthase [KO:K22847] [EC:2.8.5.1]

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