Canmetcon
Identification
Name:Cystathionine beta-lyase metC
Synonyms:
  • CBL
  • Beta-cystathionase
  • Cysteine lyase
Gene Name:metC
Enzyme Class:
Biological Properties
General Function:Involved in pyridoxal phosphate binding
Specific Function:L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb+Thumb
Thumb+Thumb+Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
ThumbThumb+Thumb+Thumb
ThumbThumb+Homocysteine+Thumb+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB036092-Aminoacrylic acidMetaboCard
ECMDB241982-aminoprop-2-enoateMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB21649CystathionineMetaboCard
ECMDB24053HomocysteineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB03276Hydrogen sulfideMetaboCard
ECMDB00099L-CystathionineMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB00192L-CystineMetaboCard
ECMDB00165L-HomocysteineMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB06343SelenocystathionineMetaboCard
ECMDB21010SelenohomocysteineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
carbon-sulfur lyase activity
catalytic activity
cofactor binding
cystathionine beta-lyase activity
lyase activity
pyridoxal phosphate binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b3008
Gene OrientationClockwise
Centisome Percentage:67.90
Left Sequence End3150258
Right Sequence End3151445
Gene Sequence:
>1188 bp
ATGAACTTATCCCTACGACGCTCTACCAGCGCCCTTCTTGCCTCGTCGTTGTTATTAACC
ATCGGACGCGGCGCTACGCTGCCATTTATGACCATTTACTTGAGTCGCCAGTACAGCCTG
AGTGTCGATCTAATCGGTTATGCGATGACAATTGCGCTCACTATTGGCGTCGTTTTTAGC
CTCGGTTTTGGTATCCTGGCGGATAAGTTCGACAAGAAACGCTATATGTTACTGGCAATT
ACCGCCTTCGCCAGCGGTTTTATTGCCATTACTTTAGTGAATAACGTGACGCTGGTTGTG
CTCTTTTTTGCCCTCATTAACTGCGCCTATTCTGTTTTTGCTACCGTGCTGAAAGCCTGG
TTTGCCGACAATCTTTCGTCCACCAGCAAAACGAAAATCTTCTCAATCAACTACACCATG
CTAAACATTGGCTGGACCATCGGTCCGCCGCTCGGCACGCTGTTGGTAATGCAGAGCATC
AATCTGCCCTTCTGGCTGGCAGCTATCTGTTCCGCGTTTCCCATGCTTTTCATTCAAATT
TGGGTAAAGCGCAGCGAGAAAATCATCGCCACGGAAACAGGCAGTGTCTGGTCGCCGAAA
GTTTTATTACAAGATAAAGCACTGTTGTGGTTTACCTGCTCTGGTTTTCTGGCTTCTTTT
GTAAGCGGCGCATTTGCTTCATGCATTTCACAATATGTGATGGTGATTGCTGATGGGGAT
TTTGCCGAAAAGGTGGTCGCGGTTGTTCTTCCGGTGAATGCTGCCATGGTGGTTACGTTG
CAATATTCCGTGGGCCGCCGACTTAACCCGGCTAACATCCGCGCGCTGATGACAGCAGGC
ACCCTCTGTTTCGTCATCGGTCTGGTCGGTTTTATTTTTTCCGGCAACAGCCTGCTATTG
TGGGGTATGTCAGCTGCGGTATTTACTGTCGGTGAAATCATTTATGCGCCGGGCGAGTAT
ATGTTGATTGACCATATTGCGCCGCCAGAAATGAAAGCCAGCTATTTTTCCGCCCAGTCT
TTAGGCTGGCTTGGTGCCGCGATTAACCCATTAGTGAGTGGCGTAGTGCTAACCAGCCTG
CCGCCTTCCTCGCTGTTTGTCATCTTAGCGTTGGTGATCATTGCTGCGTGGGTGCTGATG
TTAAAAGGGATTCGAGCAAGACCGTGGGGGCAGCCCGCGCTTTGTTGA
Protein Properties
Pfam Domain Function:
Protein Residues:395
Protein Molecular Weight:43212
Protein Theoretical pI:6
PDB File:1CL2
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cystathionine beta-lyase metC
MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRG
TLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSK
ILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDA
IIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLM
GQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFW
KRDFTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPEHIAAIRP
QGEIDFSGTLIRLHIGLEDVDDLIADLDAGFARIV
References
External Links:
ResourceLink
Uniprot ID:P06721
Uniprot Name:METC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675012
PDB ID:1CL2
Ecogene ID:EG10583
Ecocyc:EG10583
ColiBase:b3008
Kegg Gene:b3008
EchoBASE ID:EB0578
CCDB:METC_ECOLI
BacMap:16130906
General Reference:
  • Belfaiza, J., Parsot, C., Martel, A., de la Tour, C. B., Margarita, D., Cohen, G. N., Saint-Girons, I. (1986). "Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region." Proc Natl Acad Sci U S A 83:867-871. Pubmed: 3513164
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Clausen, T., Huber, R., Laber, B., Pohlenz, H. D., Messerschmidt, A. (1996). "Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A." J Mol Biol 262:202-224. Pubmed: 8831789
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Martel, A., Bouthier de la Tour, C., Le Goffic, F. (1987). "Pyridoxal 5'phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase comparison of their sequences." Biochem Biophys Res Commun 147:565-571. Pubmed: 3307782