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Protein
Submitted name:

Methionine gamma-lyase

Gene

megL

Organism
Citrobacter freundii
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

LyaseImported

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BRENDAi4.4.1.11. 1398.

Names & Taxonomyi

Protein namesi
Submitted name:
Methionine gamma-lyaseImported
Gene namesi
Name:megLImported
OrganismiCitrobacter freundiiImported
Taxonomic identifieri546 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101N6-(pyridoxal phosphate)lysineUniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4IX-ray1.90A1-398[»]
2RFVX-ray1.35A1-398[»]
3JW9X-ray1.80A1-398[»]
3JWAX-ray1.45A1-398[»]
3JWBX-ray1.63A1-398[»]
3MKJX-ray1.65A1-398[»]
4HF8X-ray2.45A1-398[»]
4MKJX-ray1.85A1-398[»]
4MKKX-ray1.45A1-398[»]
4OMAX-ray1.60A1-398[»]
ProteinModelPortaliQ84AR1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ84AR1.

Family & Domainsi

Sequence similaritiesi

Belongs to the trans-sulfuration enzymes family.UniRule annotation

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR006237. Met_gamma_lys.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11808. PTHR11808. 1 hit.
PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFiPIRSF001434. CGS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01328. met_gam_lyase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q84AR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDCRTYGFN TQIVHAGQQP DPSTGALSTP IFQTSTFVFD SAEQGAARFA
60 70 80 90 100
LEESGYIYTR LGNPTTDALE KKLAVLERGE AGLATASGIS AITTTLLTLC
110 120 130 140 150
QQGDHIVSAS AIYGCTHAFL SHSMPKFGIN VRLVDAGKPE EIRAAMRPET
160 170 180 190 200
KVVYIETPAN PTLSLVDIET VAGIAHQQGA LLVVDNTFMS PYCQQPLQLG
210 220 230 240 250
ADIVVHSVTK YINGHGDVIG GIIVGKQEFI DQARFVGLKD ITGGCMSPFN
260 270 280 290 300
AWLTLRGVKT LGIRMERHCE NALKIARFLE GHPSITRVYY PGLSSHPQYE
310 320 330 340 350
LGQRQMSLPG GIISFEIAGG LEAGRRMINS VELCLLAVSL GDTETLIQHP
360 370 380 390
ASMTHSPVAP EERLKAGITD GLIRLSVGLE DPEDIINDLE HAIRKATF
Length:398
Mass (Da):42,915
Last modified:June 1, 2003 - v1
Checksum:i915176498E76A125
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY204910 Genomic DNA. Translation: AAO46884.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY204910 Genomic DNA. Translation: AAO46884.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4IX-ray1.90A1-398[»]
2RFVX-ray1.35A1-398[»]
3JW9X-ray1.80A1-398[»]
3JWAX-ray1.45A1-398[»]
3JWBX-ray1.63A1-398[»]
3MKJX-ray1.65A1-398[»]
4HF8X-ray2.45A1-398[»]
4MKJX-ray1.85A1-398[»]
4MKKX-ray1.45A1-398[»]
4OMAX-ray1.60A1-398[»]
ProteinModelPortaliQ84AR1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.4.1.11. 1398.

Miscellaneous databases

EvolutionaryTraceiQ84AR1.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR006237. Met_gamma_lys.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11808. PTHR11808. 1 hit.
PfamiPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFiPIRSF001434. CGS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01328. met_gam_lyase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
  2. "A gene encoding L-methionine gamma-lyase is present in Enterobacteriaceae family genomes: identification and characterization of Citrobacter freundii L-methionine gamma-lyase."
    Manukhov I.V., Mamaeva D.V., Rastorguev S.M., Faleev N.G., Morozova E.A., Demidkina T.V., Zavilgelsky G.B.
    J. Bacteriol. 187:3889-3893(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "High-resolution structure of methionine gamma-lyase from Citrobacter freundii."
    Nikulin A., Revtovich S., Morozova E., Nevskaya N., Nikonov S., Garber M., Demidkina T.
    Acta Crystallogr. D 64:211-218(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
  4. "Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates."
    Revtovich S.V., Morozova E.A., Khurs E.N., Zakomirdina L.N., Nikulin A.D., Demidkina T.V., Khomutov R.M.
    Biochemistry (Mosc.) 76:564-570(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
  5. "Exploring methionine gamma-lyase structure-function relationship via microspectrophotometry and X-ray crystallography."
    Ronda L., Bazhulina N.P., Morozova E.A., Revtovich S.V., Chekhov V.O., Nikulin A.D., Demidkina T.V., Mozzarelli A.
    Biochim. Biophys. Acta 1814:834-842(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
  6. "Alliin is a suicide substrate of Citrobacter freundii methionine gamma-lyase: structural bases of inactivation of the enzyme."
    Morozova E.A., Revtovich S.V., Anufrieva N.V., Kulikova V.V., Nikulin A.D., Demidkina T.V.
    Acta Crystallogr. D 70:3034-3042(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
  7. "Crystal structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with glycine provides insight in mechanisms of two stages of physiological reaction and isotope exchange of alpha- and beta-protons of competitive inhibitors."
    Revtovich S.V., Faleev N.G., Morozova E.A., Anufrieva N.V., Nikulin A.D., Demidkina T.V.
    Biochimie 101:161-167(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
  8. "Pre-steady-state kinetic and structural analysis of interaction of methionine gamma-lyase from Citrobacter freundii with inhibitors."
    Kuznetsov N.A., Faleev N.G., Kuznetsova A.A., Morozova E.A., Revtovich S.V., Anufrieva N.V., Nikulin A.D., Fedorova O.S., Demidkina T.V.
    J. Biol. Chem. 290:671-681(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).

Entry informationi

Entry nameiQ84AR1_CITFR
AccessioniPrimary (citable) accession number: Q84AR1
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: February 17, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.