KEGG PATHWAY: pmoa00270

PATHWAY: pmoa00270

Entry

pmoa00270                   Pathway

Name

Cysteine and methionine metabolism - Passer montanus (Eurasian tree sparrow)

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

pmoa00270

Cysteine and methionine metabolism

Module

pmoa_M00034

Methionine salvage pathway [PATH:pmoa00270]

pmoa_M00035

Methionine degradation [PATH:pmoa00270]

pmoa_M00338

Cysteine biosynthesis, homocysteine + serine => cysteine [PATH:pmoa00270]

Other DBs

GO:	0006534 0006555

Organism

Passer montanus (Eurasian tree sparrow) [GN:pmoa]

Gene

120502927

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

120502929

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

120510825

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

120507390

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

120511826

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

120511828

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

120502442

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

120501193

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

120498566

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

120505022

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

120507276

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

120510561

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

120496787

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

120504616

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

120513614

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

120505826

LACC1; purine nucleoside phosphorylase LACC1 [KO:K05810] [EC:2.4.2.1 2.4.2.28 3.5.4.4]

120506086

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

120511412

methylthioribulose-1-phosphate dehydratase isoform X1 [KO:K08964] [EC:4.2.1.109]

120502724

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

120505295

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

120496190

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

120503973

IL4I1; L-amino-acid oxidase [KO:K03334] [EC:1.4.3.2]

120500924

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

120505094

DNA (cytosine-5)-methyltransferase 1-like [KO:K00558] [EC:2.1.1.37]

120508188

DNA (cytosine-5)-methyltransferase 1-like [KO:K00558] [EC:2.1.1.37]

120502931

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

120507026

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

120503056

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

120511314

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

120502254

AHCYL1; S-adenosylhomocysteine hydrolase-like protein 1 isoform X1 [KO:K01251] [EC:3.13.2.1]

120497131

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

120502503

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

120510378

GCLC; glutamate--cysteine ligase catalytic subunit isoform X1 [KO:K11204] [EC:6.3.2.2]

120510808

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

120511285

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

120512620

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

120502110

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

120508053

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

120509991

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

120509992

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

120501243

L-lactate dehydrogenase A chain isoform X1 [KO:K00016] [EC:1.1.1.27]

120507599

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

120506819

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

120507832

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

120510322

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

120497598

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

120512045

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