Q9SGU9 (MGL_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 74.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Methionine gamma-lyase Short name=AtMGL EC=4.4.1.11 Alternative name(s): L-methioninase | ||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 441 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the degradation of L-methionine to alpha-ketobutyrate, methanethiol and ammonia. Exhibits a high activity toward L-methionine, L-ethionine, L-homocysteine and seleno-L-methionine, but not L-cysteine. Involved in an alternative cysteine biosynthesis pathway to the reverse trans-sulfuration pathway (methionine->homocysteine->cystathionine->cysteine) in which methanethiol is an intermediate. Mediates also an alternative isoleucine biosynthesis pathway in which 2-ketobutyrate is an intermediate. Ref.6 Ref.7 |
| Catalytic activity | L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate. Ref.5 Ref.6 |
| Cofactor | Pyridoxal phosphate By similarity. |
| Subunit structure | Homotetramer. Ref.6 |
| Subcellular location | |
| Tissue specificity | Expressed in roots, stems, siliques, leaves, flowers and seeds after imbibition (at protein level). Transcripts accumulate in dry mature seeds, but at protein level, only present upon imbibition. Ref.5 Ref.6 |
| Induction | By sulfate deprivation and high methionine levels. Up-regulated by drought. Ref.5 Ref.6 Ref.7 |
| Disruption phenotype | Increased leaves, flowers and seeds methionine content, and leaf and root S-methylmethionine content under conditions of sulfate starvation. Reduced MGL-mediated isoleucine biosynthesis from methionine. Ref.6 Ref.7 |
| Sequence similarities | Belongs to the trans-sulfuration enzymes family. |
| Biophysicochemical properties | Absorption: Kinetic parameters: kcat is 9.5 sec(-1) with L-methionine as substrate, 8.9 sec(-1) with L-ethionine as substrate, 36.2 sec(-1) with L-homocysteine as substrate and 11.6 sec(-1) with seleno-L-methionine as substrate (Ref.6, at pH 8 and 30 degrees Celsius). KM=10 mM for L-methionine (Ref.5, at pH 7.2 and 30 degrees Celsius) KM=72 mM for L-methionine (Ref.6, at pH 8 and 30 degrees Celsius) KM=14 mM for L-ethionine (Ref.6, at pH 8 and 30 degrees Celsius) KM=92 mM for L-homocysteine (Ref.6, at pH 8 and 30 degrees Celsius) KM=40 mM for seleno-L-methionine (Ref.6, at pH 8 and 30 degrees Celsius) Vmax=194 nmol/min/mg enzyme with L-methionine as substrate (Ref.6, at pH 8 and 30 degrees Celsius) Vmax=182 nmol/min/mg enzyme with L-ethionine as substrate (Ref.6, at pH 8 and 30 degrees Celsius) Vmax=743 nmol/min/mg enzyme with L-homocysteine as substrate (Ref.6, at pH 8 and 30 degrees Celsius) Vmax=238 nmol/min/mg enzyme with seleno-L-methionine as substrate (Ref.6, at pH 8 and 30 degrees Celsius) |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cellular response to sulfate starvation Inferred from expression pattern Ref.6. Source: UniProtKB cellular response to water deprivationInferred from expression pattern Ref.7. Source: UniProtKB methionine catabolic process via 2-oxobutanoateTraceable author statement Ref.5. Source: TAIR protein homotetramerizationInferred from direct assay Ref.6. Source: UniProtKB |
| Cellular_component | cytosol Inferred from direct assay Ref.5. Source: TAIR |
| Molecular_function | methionine gamma-lyase activity Inferred from direct assay Ref.6. Source: UniProtKB pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. Davis R.W.Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [2] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| [3] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [4] | "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. Shinozaki K.Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [5] | "Methionine catabolism in Arabidopsis cells is initiated by a gamma-cleavage process and leads to S-methylcysteine and isoleucine syntheses." Rebeille F., Jabrin S., Bligny R., Loizeau K., Gambonnet B., Van Wilder V., Douce R., Ravanel S. Proc. Natl. Acad. Sci. U.S.A. 103:15687-15692(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY HIGH MET LEVELS, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. |
| [6] | "Functional characterization of a methionine gamma-lyase in Arabidopsis and its implication in an alternative to the reverse trans-sulfuration pathway." Goyer A., Collakova E., Shachar-Hill Y., Hanson A.D. Plant Cell Physiol. 48:232-242(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY SULFATE DEPRIVATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. Strain: cv. Columbia. |
| [7] | "Arabidopsis methionine gamma-lyase is regulated according to isoleucine biosynthesis needs but plays a subordinate role to threonine deaminase." Joshi V., Jander G. Plant Physiol. 151:367-378(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY DROUGHT. Strain: cv. Columbia. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC009519 Genomic DNA. Translation: AAF19680.1. CP002684 Genomic DNA. Translation: AEE34271.1. AF428413 mRNA. Translation: AAL16181.1. AY054546 mRNA. Translation: AAK96737.1. BT006588 mRNA. Translation: AAP31932.1. AK226375 mRNA. Translation: BAE98522.1. |
| IPI | IPI00518615. |
| PIR | G96669. |
| RefSeq | NP_176647.1. NM_105141.2. |
| UniGene | At.16566. At.35974. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GC0 based on UniProtKB P13254. |
| ProteinModelPortal | Q9SGU9. |
| SMR | Q9SGU9. Positions 43-422. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 3702.AT1G64660.1-P. |
Proteomic databases | |
| PaxDb | Q9SGU9. |
| PRIDE | Q9SGU9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT1G64660.1; AT1G64660.1; AT1G64660. |
| GeneID | 842774. |
| KEGG | ath:AT1G64660. |
Organism-specific databases | |
| TAIR | At1g64660. |
Phylogenomic databases | |
| eggNOG | COG0626. |
| HOGENOM | HOG000246415. |
| InParanoid | Q9SGU9. |
| KO | K01761. |
| OMA | FIDATRM. |
| PhylomeDB | Q9SGU9. |
| ProtClustDB | PLN02242. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:AT1G64660-MONOMER. |
Gene expression databases | |
| Genevestigator | Q9SGU9. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 1 hit. |
| InterPro | IPR000277. Cys/Met-Metab_PyrdxlP-dep_enz. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| PANTHER | PTHR11808. PTHR11808. 1 hit. |
| Pfam | PF01053. Cys_Met_Meta_PP. 1 hit. [Graphical view] |
| PIRSF | PIRSF001434. CGS. 1 hit. |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| PROSITE | PS00868. CYS_MET_METAB_PP. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MGL_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9SGU9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
