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Reviewed, UniProtKB/Swiss-Prot P13254 (MEGL_PSEPU)

Last modified May 26, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Methionine gamma-lyase
    EC=4.4.1.11
Alternative name(s):
    L-methioninase
Gene names
Name: mdeA
OrganismPseudomonas putida
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate.

Cofactor

Pyridoxal phosphate.

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

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Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processamino acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmethionine gamma-lyase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Methionine gamma-lyase
PRO_0000114784

Amino acid modifications

Modified residue2111N6-(pyridoxal phosphate)lysine

Secondary structure

1 ......................................................................... 398
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P13254-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: BD50CD1F34CD71E3

FASTA39842,627
        10         20         30         40         50         60 
MHGSNKLPGF ATRAIHHGYD PQDHGGALVP PVYQTATFTF PTVEYGAACF AGEQAGHFYS 

        70         80         90        100        110        120 
RISNPTLNLL EARMASLEGG EAGLALASGM GAITSTLWTL LRPGDEVLLG NTLYGCTFAF 

       130        140        150        160        170        180 
LHHGIGEFGV KLRHVDMADL QALEAAMTPA TRVIYFESPA NPNMHMADIA GVAKIARKHG 

       190        200        210        220        230        240 
ATVVVDNTYC TPYLQRPLEL GADLVVHSAT KYLSGHGDIT AGIVVGSQAL VDRIRLQGLK 

       250        260        270        280        290        300 
DMTGAVLSPH DAALLMRGIK TLNLRMDRHC ANAQVLAEFL ARQPQVELIH YPGLASFPQY 

       310        320        330        340        350        360 
TLARQQMSQP GGMIAFELKG GIGAGRRFMN ALQLFSRAVS LGDAESLAQH PASMTHSSYT 

       370        380        390 
PEERAHYGIS EGLVRLSVGL EDIDDLLADV QQALKASA

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References

[1]"Structural analysis of the L-methionine gamma-lyase gene from Pseudomonas putida."
Inoue H., Sugimoto M., Inagaki K., Esaki N., Soda K., Tanaka H.
J. Biochem. 117:1120-1125(1995) [PubMed: 8586629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ICR 3460.
[2]"Molecular characterization of the mde operon involved in L-methionine catabolism of Pseudomonas putida."
Inoue H., Inagaki K., Eriguchi S.I., Tamura T., Esaki N., Soda K., Tanaka H.
J. Bacteriol. 179:3956-3962(1997) [PubMed: 9190812] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ICR 3460.
[3]"Specific labeling of the essential cysteine residue of L-methionine gamma-lyase with a cofactor analogue, N-(bromoacetyl)pyridoxamine phosphate."
Nakayama T., Esaki N., Tanaka H., Soda K.
Biochemistry 27:1587-1591(1988) [PubMed: 3365412] [Abstract]
Cited for: PROTEIN SEQUENCE OF 91-137 AND 167-213, PYRIDOXAL PHOSPHATE AT LYS-211.
+Additional computationally mapped references.

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Cross-references

Sequence databases

D88554 Genomic DNA. Translation: BAA13642.1.
D89015 Genomic DNA. Translation: BAA20553.1.
PIRA27691.
JC4174.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GC0X-ray1.70A/B/C/D1-398[»]
1GC2X-ray2.00A/B/C/D1-398[»]
1PG8X-ray2.68A/B/C/D1-398[»]
1UKJX-ray1.80A/B/C/D1-398[»]
2O7CX-ray1.70A/B/C/D1-398[»]
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MON-284.
BRENDA4.4.1.11. 403.

Family and domain databases

InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR006237. Met_gamma_lys.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PANTHERPTHR11808. Cys_Met_Meta_PP. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
TIGRFAMsTIGR01328. met_gam_lyase. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMEGL_PSEPU
AccessionPrimary (citable) accession number: P13254
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1996
Last modified: May 26, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents