Serine hydroxymethyltransferase (P0A825)

Identification
Name:Serine hydroxymethyltransferase
Synonyms:
  • SHMT
  • Serine methylase
Gene Name:glyA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Interconversion of serine and glycine
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Threonine ↔ 1.0Acetaldehyde + 1.0Glycine
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Allothreonine → 1.0Acetaldehyde + 1.0Glycine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Serine + 1.0Tetrahydrofolic acid ↔ 1.0Glycine + 1.0Water + 1.05,10-Methylene-THF
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N5-Formyl-H4F + 1.0Hydrogen ion → 1.0Water + 1.05,10-Methenyltetrahydrofolate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0Glycine + 1.0Water ↔ 1.0Tetrahydrofolic acid + 1.0L-Serine
ReactionCard
1.0Thumb+1.05,6,7,8-Tetrahydromethanopterin ↔ 1.05,10-Methylenetetrahydromethanopterin+1.0Thumb+1.0Thumb
1.0L-Serine + 1.05,6,7,8-Tetrahydromethanopterin ↔ 1.05,10-Methylenetetrahydromethanopterin + 1.0Glycine + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Tetrahydrofolic acid+1.0L-Serine+1.0Thumb+1.0Thumb ↔ 1.05,10-Methylene-THF+1.0Thumb+1.0Thumb+1.0Thumb
1.0Tetrahydrofolic acid + 1.0L-Serine + 1.0Tetrahydrofolic acid + 1.0L-Serine ↔ 1.05,10-Methylene-THF + 1.0Glycine + 1.0Water + 1.05,10-Methylene-THF
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Threonine ↔ 1.0Acetaldehyde + 1.0Glycine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0D-Alanine + 1.0Pyridoxal 5'-phosphate → 1.0Pyridoxamine 5'-phosphate + 1.0Pyruvic acid
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Allothreonine → 1.0Acetaldehyde + 1.0Glycine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Serine + 1.0Tetrahydrofolic acid ↔ 1.0Glycine + 1.0Water + 1.05,10-Methylene-THF
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N5-Formyl-H4F + 1.0Hydrogen ion → 1.0Water + 1.05,10-Methenyltetrahydrofolate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0Glycine + 1.0Water ↔ 1.0Tetrahydrofolic acid + 1.0L-Serine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Alanine + 1.0Pyridoxal 5'-phosphate → 1.0Pyridoxamine 5'-phosphate + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.05,10-Methenyltetrahydrofolate → 1.0N5-Formyl-H4F + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.05,10-Methylene-THF + 1.0Glycine + 1.0Water → 1.0Tetrahydrofolic acid + 1.0L-Serine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211765,10-MethenyltetrahydrofolateMetaboCard
ECMDB013545,10-Methylene-THFMetaboCard
ECMDB00990AcetaldehydeMetaboCard
ECMDB01310D-AlanineMetaboCard
ECMDB00123GlycineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00161L-AlanineMetaboCard
ECMDB21007L-AllothreonineMetaboCard
ECMDB00187L-SerineMetaboCard
ECMDB00167L-ThreonineMetaboCard
ECMDB01562N5-Formyl-H4FMetaboCard
ECMDB01491Pyridoxal 5'-phosphateMetaboCard
ECMDB01555Pyridoxamine 5'-phosphateMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB01846Tetrahydrofolic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cofactor binding
glycine hydroxymethyltransferase activity
methyltransferase activity
pyridoxal phosphate binding
transferase activity
transferase activity, transferring one-carbon groups
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
glycine metabolic process
L-serine metabolic process
metabolic process
serine family amino acid metabolic process
Gene Properties
Blattner:b2551
Gene OrientationCounterclockwise
Centisome Percentage:57.81
Left Sequence End2682276
Right Sequence End2683529
Gene Sequence:
>1254 bp
ATGCTGGAACAAATGGGCATTGCCGCGAAGCAAGCCTCGTATAAATTAGCGCAACTCTCC
AGCCGCGAAAAAAATCGCGTGCTGGAAAAAATCGCCGATGAACTGGAAGCACAAAGCGAA
ATCATCCTCAACGCTAACGCCCAGGATGTTGCTGACGCGCGAGCCAATGGCCTTAGCGAA
GCGATGCTTGACCGTCTGGCACTGACGCCCGCACGGCTGAAAGGCATTGCCGACGATGTA
CGTCAGGTGTGCAACCTCGCCGATCCGGTGGGGCAGGTAATCGATGGCGGCGTACTGGAC
AGCGGCCTGCGTCTTGAGCGTCGTCGCGTACCGCTGGGGGTTATTGGCGTGATTTATGAA
GCGCGCCCGAACGTGACGGTTGATGTCGCTTCGCTGTGCCTGAAAACCGGTAATGCGGTG
ATCCTGCGCGGTGGCAAAGAAACGTGTCGCACTAACGCTGCAACGGTGGCGGTGATTCAG
GACGCCCTGAAATCCTGCGGCTTACCGGCGGGTGCCGTGCAGGCGATTGATAATCCTGAC
CGTGCGCTGGTCAGTGAAATGCTGCGTATGGATAAATACATCGACATGCTGATCCCGCGT
GGTGGCGCTGGTTTGCATAAACTGTGCCGTGAACAGTCGACAATCCCGGTGATCACAGGT
GGTATAGGCGTATGCCATATTTACGTTGATGAAAGTGTAGAGATCGCTGAAGCATTAAAA
GTGATCGTCAACGCGAAAACTCAGCGTCCGAGCACATGTAATACGGTTGAAACGTTGCTG
GTGAATAAAAACATCGCCGATAGCTTCCTGCCCGCATTAAGCAAACAAATGGCGGAAAGC
GGCGTGACATTACACGCAGATGCAGCTGCACTGGCGCAGTTGCAGGCAGGCCCTGCGAAG
GTGGTTGCTGTTAAAGCCGAAGAGTATGACGATGAGTTTCTGTCATTAGATTTGAACGTC
AAAATCGTCAGCGATCTTGACGATGCCATCGCCCATATTCGTGAACACGGCACACAACAC
TCCGATGCGATCCTGACCCGCGATATGCGCAACGCCCAGCGTTTTGTTAACGAAGTGGAT
TCGTCCGCTGTTTACGTTAACGCCTCTACGCGTTTTACCGACGGCGGCCAGTTTGGTCTG
GGTGCGGAAGTGGCGGTAAGCACACAAAAACTCCACGCGCGTGGCCCAATGGGGCTGGAA
GCACTGACCACTTACAAGTGGATCGGCATTGGTGATTACACCATTCGTGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:417
Protein Molecular Weight:45316
Protein Theoretical pI:6
PDB File:1DFO
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Serine hydroxymethyltransferase
MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYP
GKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLEPGDTVLGMN
LAHGGHLTHGSPVNFSGKLYNIVPYGIDATGHIDYADLEKQAKEHKPKMIIGGFSAYSGV
VDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLIL
AKGGSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVE
VFLERGYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTS
GIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKGKVLDICARYPVYA
References
External Links:
ResourceLink
Uniprot ID:P0A825
Uniprot Name:GLYA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674395
PDB ID:1DFO
Ecogene ID:EG10408
Ecocyc:EG10408
ColiBase:b2551
Kegg Gene:b2551
EchoBASE ID:EB0403
CCDB:GLYA_ECOLI
BacMap:16130476
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
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Plamann, M. D., Stauffer, G. V. (1983). "Characterization of the Escherichia coli gene for serine hydroxymethyltransferase." Gene 22:9-18. Pubmed: 6190704
  • Plamann, M. D., Stauffer, L. T., Urbanowski, M. L., Stauffer, G. V. (1983). "Complete nucleotide sequence of the E. coli glyA gene." Nucleic Acids Res 11:2065-2075. Pubmed: 6300791
  • Scarsdale, J. N., Radaev, S., Kazanina, G., Schirch, V., Wright, H. T. (2000). "Crystal structure at 2.4 A resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate." J Mol Biol 296:155-168. Pubmed: 10656824
  • Vasudevan, S. G., Armarego, W. L., Shaw, D. C., Lilley, P. E., Dixon, N. E., Poole, R. K. (1991). "Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12." Mol Gen Genet 226:49-58. Pubmed: 2034230
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842