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P06721 (METC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystathionine beta-lyase MetC

Short name=CBL
EC=4.4.1.8
Alternative name(s):
Beta-cystathionase
Cysteine lyase
Gene names
Name:metC
Ordered Locus Names:b3008, JW2975
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-cystathionine + H2O = L-homocysteine + NH3 + pyruvate.

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.

Subunit structure

Homotetramer. Ref.6

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the trans-sulfuration enzymes family.

Sequence caution

The sequence AAA69175.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Cystathionine beta-lyase MetC
PRO_0000114768

Amino acid modifications

Modified residue2101N6-(pyridoxal phosphate)lysine

Secondary structure

..................................................................... 395
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06721 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: FD3308423D6427C6

FASTA39543,212
        10         20         30         40         50         60 
MADKKLDTQL VNAGRSKKYT LGAVNSVIQR ASSLVFDSVE AKKHATRNRA NGELFYGRRG 

        70         80         90        100        110        120 
TLTHFSLQQA MCELEGGAGC VLFPCGAAAV ANSILAFIEQ GDHVLMTNTA YEPSQDFCSK 

       130        140        150        160        170        180 
ILSKLGVTTS WFDPLIGADI VKHLQPNTKI VFLESPGSIT MEVHDVPAIV AAVRSVVPDA 

       190        200        210        220        230        240 
IIMIDNTWAA GVLFKALDFG IDVSIQAATK YLVGHSDAMI GTAVCNARCW EQLRENAYLM 

       250        260        270        280        290        300 
GQMVDADTAY ITSRGLRTLG VRLRQHHESS LKVAEWLAEH PQVARVNHPA LPGSKGHEFW 

       310        320        330        340        350        360 
KRDFTGSSGL FSFVLKKKLN NEELANYLDN FSLFSMAYSW GGYESLILAN QPEHIAAIRP 

       370        380        390 
QGEIDFSGTL IRLHIGLEDV DDLIADLDAG FARIV 

« Hide

References

« Hide 'large scale' references
[1]"Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region."
Belfaiza J., Parsot C., Martel A., de la Tour C.B., Margarita D., Cohen G.N., Saint-Girons I.
Proc. Natl. Acad. Sci. U.S.A. 83:867-871(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences."
Martel A., Bouthier de la Tour C., Le Goffic F.
Biochem. Biophys. Res. Commun. 147:565-571(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 194-221.
[5]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[6]"Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A."
Clausen T., Huber R., Laber B., Pohlenz H.-D., Messerschmidt A.
J. Mol. Biol. 262:202-224(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-210.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12858 Genomic DNA. Translation: AAA24158.1.
U28377 Genomic DNA. Translation: AAA69175.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76044.1.
AP009048 Genomic DNA. Translation: BAE77065.1.
PIRWZECCB. A25153.
RefSeqNP_417481.1. NC_000913.3.
YP_491201.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CL1X-ray1.83A/B1-395[»]
1CL2X-ray2.20A/B1-395[»]
2FQ6X-ray1.78A/B1-395[»]
2GQNX-ray1.80A/B1-395[»]
ProteinModelPortalP06721.
SMRP06721. Positions 4-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10193N.
IntActP06721. 6 interactions.
STRING511145.b3008.

Chemistry

ChEMBLCHEMBL1075079.

Proteomic databases

PaxDbP06721.
PRIDEP06721.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76044; AAC76044; b3008.
BAE77065; BAE77065; BAE77065.
GeneID12932425.
946240.
KEGGecj:Y75_p2935.
eco:b3008.
PATRIC32121430. VBIEscCol129921_3102.

Organism-specific databases

EchoBASEEB0578.
EcoGeneEG10583. metC.

Phylogenomic databases

eggNOGCOG0626.
HOGENOMHOG000246416.
KOK01760.
OMAEQSYLMG.
OrthoDBEOG67DPN3.
PhylomeDBP06721.

Enzyme and pathway databases

BioCycEcoCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
ECOL316407:JW2975-MONOMER.
MetaCyc:CYSTATHIONINE-BETA-LYASE-MONOMER.
UniPathwayUPA00051; UER00078.

Gene expression databases

GenevestigatorP06721.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR000277. Cys/Met-Metab_PyrdxlP-dep_enz.
IPR006233. Cys_b_lyase_bac.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11808. PTHR11808. 1 hit.
PfamPF01053. Cys_Met_Meta_PP. 1 hit.
[Graphical view]
PIRSFPIRSF001434. CGS. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01324. cysta_beta_ly_B. 1 hit.
PROSITEPS00868. CYS_MET_METAB_PP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06721.
PROP06721.

Entry information

Entry nameMETC_ECOLI
AccessionPrimary (citable) accession number: P06721
Secondary accession number(s): Q2M9J1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 11, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene