KEGG PATHWAY: bkw00270

PATHWAY: bkw00270

Entry

bkw00270                    Pathway

Name

Cysteine and methionine metabolism - Halalkalibacter krulwichiae

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

bkw00270

Cysteine and methionine metabolism

Module

bkw_M00017

Methionine biosynthesis, aspartate => homoserine => methionine [PATH:bkw00270]

bkw_M00021

Cysteine biosynthesis, serine => cysteine [PATH:bkw00270]

bkw_M00034

Methionine salvage pathway [PATH:bkw00270]

Other DBs

GO:	0006534 0006555

Organism

Halalkalibacter krulwichiae [GN:bkw]

Gene

BkAM31D_00610

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

BkAM31D_19095

cysK_2; Cysteine synthase [KO:K01738] [EC:2.5.1.47]

BkAM31D_00460

cysK_1; Cysteine synthase [KO:K01738] [EC:2.5.1.47]

BkAM31D_19280

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

BkAM31D_10860

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

BkAM31D_10855

yitJ; Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase [KO:K24042] [EC:2.1.1.13 1.5.1.54]

BkAM31D_10640

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

BkAM31D_19200

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

BkAM31D_18595

speH; S-adenosylmethionine decarboxylase proenzyme precursor [KO:K01611] [EC:4.1.1.50]

BkAM31D_11915

speD; S-adenosylmethionine decarboxylase proenzyme precursor [KO:K01611] [EC:4.1.1.50]

BkAM31D_24705

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

BkAM31D_18940

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

BkAM31D_06385

mtnK; Methylthioribose kinase [KO:K00899] [EC:2.7.1.100]

BkAM31D_15190

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

BkAM31D_04955

mtaD_1; 5-methylthioadenosine/S-adenosylhomocysteine deaminase [KO:K12960] [EC:3.5.4.31 3.5.4.28]

BkAM31D_13175

mtaD_2; 5-methylthioadenosine/S-adenosylhomocysteine deaminase [KO:K12960] [EC:3.5.4.31 3.5.4.28]

BkAM31D_06380

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

BkAM31D_06405

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

BkAM31D_06395

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

BkAM31D_06400

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

BkAM31D_06410

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

BkAM31D_04210

dapL_1; LL-diaminopimelate aminotransferase [KO:K08969] [EC:2.6.1.117]

BkAM31D_14135

mdeA_2; Methionine gamma-lyase [KO:K01761] [EC:4.4.1.11]

BkAM31D_18895

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

BkAM31D_04960

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

BkAM31D_18400

lysC_2; Aspartokinase [KO:K00928] [EC:2.7.2.4]

BkAM31D_14495

lysC_1; Aspartokinase 2 [KO:K00928] [EC:2.7.2.4]

BkAM31D_06070

yclM; Aspartokinase 3 [KO:K00928] [EC:2.7.2.4]

BkAM31D_14500

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

BkAM31D_11435

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

BkAM31D_19910

hom_3; Homoserine dehydrogenase [KO:K00003] [EC:1.1.1.3]

BkAM31D_04790

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

BkAM31D_13775

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

BkAM31D_11425

mccB; Cystathionine gamma-lyase [KO:K01739] [EC:2.5.1.48]

BkAM31D_10850

metI; Cystathionine gamma-synthase/O-acetylhomoserine (thiol)-lyase [KO:K01739] [EC:2.5.1.48]

BkAM31D_18305

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

BkAM31D_13120

ilvK; Branched-chain-amino-acid aminotransferase 2 [KO:K00826] [EC:2.6.1.42]

BkAM31D_23185

gshAB_2; Glutathione biosynthesis bifunctional protein GshAB [KO:K01919] [EC:6.3.2.2]

BkAM31D_11200

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

BkAM31D_19400

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

BkAM31D_05710

ldhP; L-lactate dehydrogenase P [KO:K00016] [EC:1.1.1.27]

BkAM31D_10430

ldh1_2; L-lactate dehydrogenase 1 [KO:K00016] [EC:1.1.1.27]

BkAM31D_18650

mdh_3; Malate dehydrogenase [KO:K00024] [EC:1.1.1.37]

BkAM31D_02825

ldh1_1; L-lactate dehydrogenase 1 [KO:K00024] [EC:1.1.1.37]

BkAM31D_21940

ldhA; L-lactate dehydrogenase 1 [KO:K00024] [EC:1.1.1.37]

BkAM31D_14965

sdhA; L-serine dehydratase, alpha chain [KO:K01752] [EC:4.3.1.17]

BkAM31D_14970

sdhB; L-serine dehydratase, beta chain [KO:K01752] [EC:4.3.1.17]

BkAM31D_25050

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

BkAM31D_04475

serC_1; 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

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