KEGG PATHWAY: pano00270

PATHWAY: pano00270

Entry

pano00270                   Pathway

Name

Cysteine and methionine metabolism - Pantoea anthophila

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

pano00270

Cysteine and methionine metabolism

Module

pano_M00017

Methionine biosynthesis, aspartate => homoserine => methionine [PATH:pano00270]

pano_M00021

Cysteine biosynthesis, serine => cysteine [PATH:pano00270]

pano_M00034

Methionine salvage pathway [PATH:pano00270]

Other DBs

GO:	0006534 0006555

Organism

Pantoea anthophila [GN:pano]

Gene

OJ965_03260

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

OJ965_16390

PLP-dependent cysteine synthase family protein [KO:K01738] [EC:2.5.1.47]

OJ965_07750

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

OJ965_05750

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

OJ965_10285

PatB family C-S lyase [KO:K14155] [EC:4.4.1.13]

OJ965_06985

mmuM; homocysteine S-methyltransferase [KO:K00547] [EC:2.1.1.10]

OJ965_19665

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

OJ965_19990

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

OJ965_02020

methionine synthase [KO:K00549] [EC:2.1.1.14]

OJ965_06110

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

OJ965_17510

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

OJ965_17505

speE; polyamine aminopropyltransferase [KO:K00797] [EC:2.5.1.16]

OJ965_14310

autoinducer synthase [KO:K13061] [EC:2.3.1.184]

OJ965_17365

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

OJ965_16985

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

OJ965_05510

polyphenol oxidase family protein [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

OJ965_06870

yfiH; purine nucleoside phosphorylase YfiH [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

OJ965_16990

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

OJ965_17005

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

OJ965_17000

mtnC; acireductone synthase [KO:K09880] [EC:3.1.3.77]

OJ965_16995

acireductone dioxygenase [KO:K08967] [EC:1.13.11.53 1.13.11.54]

OJ965_19510

aspartate/tyrosine/aromatic aminotransferase [KO:K00832] [EC:2.6.1.57]

OJ965_17490

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

OJ965_10575

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

OJ965_09840

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

OJ965_06790

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

OJ965_19635

lysC; lysine-sensitive aspartokinase 3 [KO:K00928] [EC:2.7.2.4]

OJ965_17995

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

OJ965_03415

bifunctional aspartate kinase/homoserine dehydrogenase II [KO:K12525] [EC:2.7.2.4 1.1.1.3]

OJ965_04185

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

OJ965_19690

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

OJ965_03410

metB; cystathionine gamma-synthase [KO:K01739] [EC:2.5.1.48]

OJ965_03560

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

OJ965_06785

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

OJ965_06075

gshB; glutathione synthase [KO:K01920] [EC:6.3.2.3]

OJ965_14595

aspartate/tyrosine/aromatic aminotransferase [KO:K00813] [EC:2.6.1.1]

OJ965_07360

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

OJ965_00250

aspartate/glutamate racemase family protein [KO:K25316] [EC:5.1.1.10]

OJ965_00900

aspartate/glutamate racemase family protein [KO:K25316] [EC:5.1.1.10]

OJ965_10075

D-cysteine desulfhydrase [KO:K05396] [EC:4.4.1.15]

OJ965_05065

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

OJ965_10660

L-serine ammonia-lyase [KO:K01752] [EC:4.3.1.17]

OJ965_12035

pyridoxal-phosphate dependent enzyme [KO:K17989] [EC:4.3.1.17 4.3.1.19]

OJ965_07715

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

OJ965_06180

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

OJ965_02040

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

OJ965_21020

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

OJ965_21055

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

OJ965_14695

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