KEGG PATHWAY: cfir00270

PATHWAY: cfir00270

Entry

cfir00270                   Pathway

Name

Cysteine and methionine metabolism - Cytobacillus firmus

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

cfir00270

Cysteine and methionine metabolism

Module

cfir_M00017

Methionine biosynthesis, aspartate => homoserine => methionine [PATH:cfir00270]

cfir_M00021

Cysteine biosynthesis, serine => cysteine [PATH:cfir00270]

cfir_M00034

Methionine salvage pathway [PATH:cfir00270]

cfir_M00609

Cysteine biosynthesis, methionine => cysteine [PATH:cfir00270]

Other DBs

GO:	0006534 0006555

Organism

Cytobacillus firmus [GN:cfir]

Gene

NAF01_00590

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

NAF01_22895

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

NAF01_00430

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

NAF01_20355

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

NAF01_02895

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

NAF01_11760

metC; cystathionine beta-lyase [KO:K01760] [EC:4.4.1.13]

NAF01_21145

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

NAF01_22820

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

NAF01_02890

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

NAF01_11770

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

NAF01_11765

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

NAF01_20495

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

NAF01_12115

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

NAF01_19870

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

NAF01_24080

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

NAF01_15265

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

NAF01_19045

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

NAF01_04795

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

NAF01_08780

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

NAF01_11130

5'-deoxyadenosine deaminase [KO:K12960] [EC:3.5.4.31 3.5.4.28]

NAF01_04800

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

NAF01_07960

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

NAF01_07950

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

NAF01_07955

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

NAF01_11405

MtnX-like HAD-IB family phosphatase [KO:K08966] [EC:3.1.3.87]

NAF01_07965

cupin domain-containing protein [KO:K08967] [EC:1.13.11.53 1.13.11.54]

NAF01_07945

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

NAF01_20170

megL; methionine gamma-lyase [KO:K01761] [EC:4.4.1.11]

NAF01_20165

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

NAF01_02885

class I SAM-dependent methyltransferase [KO:K17462] [EC:2.1.1.-]

NAF01_20570

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

NAF01_02175

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

NAF01_09485

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

NAF01_19710

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

NAF01_09480

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

NAF01_06090

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

NAF01_21405

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

NAF01_17070

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

NAF01_11755

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

NAF01_21575

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

NAF01_11290

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

NAF01_24050

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

NAF01_17400

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

NAF01_17165

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

NAF01_18560

L-lactate dehydrogenase [KO:K00016] [EC:1.1.1.27]

NAF01_24535

L-lactate dehydrogenase [KO:K00016] [EC:1.1.1.27]

NAF01_12655

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

NAF01_19925

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

NAF01_04365

UxaA family hydrolase [KO:K16845] [EC:4.4.1.24]

NAF01_10665

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

NAF01_10670

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

NAF01_15290

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

NAF01_22335

C-terminal binding protein [KO:K00058] [EC:1.1.1.95 1.1.1.399]

NAF01_23075

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

NAF01_06680

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