KEGG PATHWAY: pvt00270

PATHWAY: pvt00270

Entry

pvt00270                    Pathway

Name

Cysteine and methionine metabolism - Pogona vitticeps (central bearded dragon)

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

pvt00270

Cysteine and methionine metabolism

Module

pvt_M00034

Methionine salvage pathway [PATH:pvt00270]

pvt_M00035

Methionine degradation [PATH:pvt00270]

pvt_M00338

Cysteine biosynthesis, homocysteine + serine => cysteine [PATH:pvt00270]

Other DBs

GO:	0006534 0006555

Organism

Pogona vitticeps (central bearded dragon) [GN:pvt]

Gene

110079859

cystathionine gamma-lyase-like [KO:K01758] [EC:4.4.1.1]

110079862

cystathionine gamma-lyase-like isoform X1 [KO:K01758] [EC:4.4.1.1]

110079452

KYAT3; kynurenine--oxoglutarate transaminase 3 isoform X1 [KO:K00816] [EC:2.6.1.7 4.4.1.13 2.6.1.64]

110079688

KYAT1; kynurenine--oxoglutarate transaminase 1 isoform X1 [KO:K00816] [EC:2.6.1.7 4.4.1.13 2.6.1.64]

110074069

cystathionine beta-synthase-like [KO:K01697] [EC:4.2.1.22]

110074034

cystathionine beta-synthase-like [KO:K01697] [EC:4.2.1.22]

110073962

BHMT; betaine--homocysteine S-methyltransferase 1 [KO:K00544] [EC:2.1.1.5]

110075749

MTR; methionine synthase isoform X1 [KO:K00548] [EC:2.1.1.13]

110086741

MAT2B; methionine adenosyltransferase 2 subunit beta [KO:K00789] [EC:2.5.1.6]

110072146

MAT2A; S-adenosylmethionine synthase [KO:K00789] [EC:2.5.1.6]

110083662

MAT1A; S-adenosylmethionine synthase [KO:K00789] [EC:2.5.1.6]

110070311

S-adenosylmethionine synthase-like isoform X1 [KO:K00789] [EC:2.5.1.6]

110085310

AMD1; S-adenosylmethionine decarboxylase proenzyme isoform X1 [KO:K01611] [EC:4.1.1.50]

110073115

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

110076724

SMS; spermine synthase isoform X1 [KO:K00802] [EC:2.5.1.22]

110077382

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

110080813

LACC1; laccase domain-containing protein 1 [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

110078720

MRI1; methylthioribose-1-phosphate isomerase [KO:K08963] [EC:5.3.1.23]

110073525

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

110083350

ENOPH1; enolase-phosphatase E1 [KO:K09880] [EC:3.1.3.77]

110073419

ADI1; 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase isoform X1 [KO:K08967] [EC:1.13.11.53 1.13.11.54]

110076298

TAT; tyrosine aminotransferase [KO:K00815] [EC:2.6.1.5]

110071372

L-amino-acid oxidase-like [KO:K03334] [EC:1.4.3.2]

110088018

L-amino-acid oxidase-like [KO:K03334] [EC:1.4.3.2]

110088019

L-amino-acid oxidase-like [KO:K03334] [EC:1.4.3.2]

110088021

LOW QUALITY PROTEIN: L-amino-acid oxidase-like [KO:K03334] [EC:1.4.3.2]

110088022

L-amino-acid oxidase-like [KO:K03334] [EC:1.4.3.2]

110087012

GNMT; glycine N-methyltransferase isoform X1 [KO:K00552] [EC:2.1.1.20]

110089202

DNMT1; DNA (cytosine-5)-methyltransferase 1 isoform X1 [KO:K00558] [EC:2.1.1.37]

110086977

DNMT3A; DNA (cytosine-5)-methyltransferase 3A isoform X1 [KO:K17398] [EC:2.1.1.37]

110086712

DNMT3B; DNA (cytosine-5)-methyltransferase 3B [KO:K17399] [EC:2.1.1.37]

110089410

AHCYL2; adenosylhomocysteinase 3 isoform X1 [KO:K01251] [EC:3.13.2.1]

110085915

AHCY; adenosylhomocysteinase isoform X1 [KO:K01251] [EC:3.13.2.1]

110087977

AHCYL1; adenosylhomocysteinase 2 isoform X1 [KO:K01251] [EC:3.13.2.1]

110090204

BCAT1; branched-chain-amino-acid aminotransferase, cytosolic isoform X1 [KO:K00826] [EC:2.6.1.42]

110078578

BCAT2; branched-chain-amino-acid aminotransferase, mitochondrial isoform X1 [KO:K00826] [EC:2.6.1.42]

110080093

AGXT2; alanine--glyoxylate aminotransferase 2, mitochondrial isoform X1 [KO:K00827] [EC:2.6.1.44 2.6.1.40]

110090238

GCLC; glutamate--cysteine ligase catalytic subunit [KO:K11204] [EC:6.3.2.2]

110076485

GCLM; glutamate--cysteine ligase regulatory subunit isoform X1 [KO:K11205]

110073348

GSS; glutathione synthetase isoform X1 [KO:K21456] [EC:6.3.2.3]

110072047

CDO1; cysteine dioxygenase type 1 [KO:K00456] [EC:1.13.11.20]

110084029

GOT1; aspartate aminotransferase, cytoplasmic [KO:K14454] [EC:2.6.1.1]

110075176

GOT1L1; putative aspartate aminotransferase, cytoplasmic 2 [KO:K14454] [EC:2.6.1.1]

110081318

GOT2; aspartate aminotransferase, mitochondrial isoform X1 [KO:K14455] [EC:2.6.1.1]

110075937

MPST; 3-mercaptopyruvate sulfurtransferase isoform X1 [KO:K01011] [EC:2.8.1.1 2.8.1.2]

110075939

TST; thiosulfate sulfurtransferase [KO:K01011] [EC:2.8.1.1 2.8.1.2]

110088549

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

110082996

LDHB; L-lactate dehydrogenase B chain [KO:K00016] [EC:1.1.1.27]

110084218

MDH1; malate dehydrogenase, cytoplasmic [KO:K00025] [EC:1.1.1.37]

110085149

MDH2; malate dehydrogenase, mitochondrial [KO:K00026] [EC:1.1.1.37]

110086277

SDSL; serine dehydratase-like [KO:K17989] [EC:4.3.1.17 4.3.1.19]

110086281

L-serine dehydratase/L-threonine deaminase-like [KO:K17989] [EC:4.3.1.17 4.3.1.19]

110071404

L-serine dehydratase/L-threonine deaminase-like [KO:K17989] [EC:4.3.1.17 4.3.1.19]

110089840

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

110076006

PSAT1; 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