Identification
Name:Cystathionine gamma-synthase
Synonyms:
  • CGS
  • O-succinylhomoserine (thiol)-lyase
Gene Name:metB
Enzyme Class:
Biological Properties
General Function:Involved in pyridoxal phosphate binding
Specific Function:O(4)-succinyl-L-homoserine + L-cysteine = L- cystathionine + succinate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
O-Phosphorylhomoserine+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+Thumb+Thumb+Thumb ? Thumb+Thumb
SMPDB Reactions:
Thumb+ThumbThumb+Thumb+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb+Thumb+Thumb ? Thumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB000052-Ketobutyric acidMetaboCard
ECMDB00042Acetic acidMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21649CystathionineMetaboCard
ECMDB00731Cysteine-S-sulfateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB03276Hydrogen sulfideMetaboCard
ECMDB00099L-CystathionineMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB00165L-HomocysteineMetaboCard
ECMDB03011O-AcetylserineMetaboCard
ECMDB01418O-Succinyl-L-homoserineMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB06343SelenocystathionineMetaboCard
ECMDB03288SelenocysteineMetaboCard
ECMDB00254Succinic acidMetaboCard
ECMDB00257ThiosulfateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cofactor binding
pyridoxal phosphate binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
Gene Properties
Blattner:b3939
Gene OrientationClockwise
Centisome Percentage:88.94
Left Sequence End4126695
Right Sequence End4127855
Gene Sequence:
>1161 bp
ATGACAAATAACCCTCTGATTCCACAAAGCAAACTTCCACAACTTGGCACCACTATTTTC
ACCCAGATGAGCGCGCTGGCGCAGCAACACCAGGCGATTAACCTGTCGCAAGGCTTTCCT
GATTTTGATGGTCCGCGCTATTTACAGGAGCGGCTGGCGCACCACGTTGCACAGGGGGCA
AACCAATACGCGCCCATGACCGGCGTGCAGGCCTTGCGCGAGGCGATTGCTCAGAAAACG
GAACGTTTGTATGGCTATCAACCAGATGCCGATAGCGATATCACCGTAACGGCAGGGGCG
ACGGAAGCGTTATACGCGGCGATTACCGCACTGGTGCGCAATGGCGATGAAGTGATTTGT
TTTGATCCCAGCTATGACAGTTACGCCCCCGCCATCGCGCTTTCTGGGGGAATAGTGAAG
CGTATGGCACTGCAACCACCGCATTTTCGCGTTGACTGGCAGGAATTTGCCGCATTATTA
AGCGAGCGCACCAGACTGGTGATCCTCAACACTCCGCATAACCCCAGTGCAACTGTCTGG
CAGCAGGCTGATTTCGCCGCTTTGTGGCAGGCGATCGCCGGGCACGAGATTTTTGTCATT
AGCGATGAAGTCTACGAGCACATCAACTTTTCACAACAGGGCCATGCCAGTGTGCTGGCG
CATCCGCAGCTGCGTGAGCGGGCAGTGGCGGTTTCTTCATTTGGCAAGACCTATCATATG
ACCGGCTGGAAAGTGGGTTATTGTGTTGCGCCAGCGCCCATCAGCGCCGAAATTCGCAAG
GTACATCAGTATCTGACCTTTTCGGTGAATACCCCGGCACAGCTGGCGCTTGCTGATATG
CTACGTGCAGAACCTGAGCATTATCTTGCGTTACCGGACTTTTATCGCCAGAAGCGCGAT
ATTCTGGTGAATGCTTTAAATGAAAGCCGGCTGGAGATTTTACCGTGTGAAGGTACATAC
TTTTTGCTGGTGGATTACAGCGCGGTTTCTACCCTGGATGATGTTGAGTTTTGCCAGTGG
CTGACGCAGGAGCACGGCGTAGCGGCGATTCCGCTGTCGGTGTTTTGCGCCGATCCCTTC
CCACATAAACTGATTCGTCTCTGTTTTGCCAAGAAGGAATCGACGTTGCTGGCAGCAGCT
GAACGCCTGCGCCAGCTTTAG
Protein Properties
Pfam Domain Function:
Protein Residues:386
Protein Molecular Weight:41550
Protein Theoretical pI:6
PDB File:1CS1
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cystathionine gamma-synthase
MTRKQATIAVRSGLNDDEQYGCVVPPIHLSSTYNFTGFNEPRAHDYSRRGNPTRDVVQRA
LAELEGGAGAVLTNTGMSAIHLVTTVFLKPGDLLVAPHDCYGGSYRLFDSLAKRGCYRVL
FVDQGDEQALRAALAEKPKLVLVESPSNPLLRVVDIAKICHLAREVGAVSVVDNTFLSPA
LQNPLALGADLVLHSCTKYLNGHSDVVAGVVIAKDPDVVTELAWWANNIGVTGGAFDSYL
LLRGLRTLVPRMELAQRNAQAIVKYLQTQPLVKKLYHPSLPENQGHEIAARQQKGFGAML
SFELDGDEQTLRRFLGGLSLFTLAESLGGVESLISHAATMTHAGMAPEARAAAGISETLL
RISTGIEDGEDLIADLENGFRAANKG
References
External Links:
ResourceLink
Uniprot ID:P00935
Uniprot Name:METB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062217
PDB ID:1CS1
Ecogene ID:EG10582
Ecocyc:EG10582
ColiBase:b3939
Kegg Gene:b3939
EchoBASE ID:EB0577
CCDB:METB_ECOLI
BacMap:16131777
General Reference:
  • 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., Prade, L., Wahl, M. C., Messerschmidt, A. (1998). "Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution." EMBO J 17:6827-6838. Pubmed: 9843488
  • Duchange, N., Zakin, M. M., Ferrara, P., Saint-Girons, I., Park, I., Tran, S. V., Py, M. C., Cohen, G. N. (1983). "Structure of the metJBLF cluster in Escherichia coli K12. Sequence of the metB structural gene and of the 5'- and 3'-flanking regions of the metBL operon." J Biol Chem 258:14868-14871. Pubmed: 6361020
  • 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
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018