Serine hydroxymethyltransferase

Details

Name
Serine hydroxymethyltransferase
Synonyms
  • 2.1.2.1
  • SHMT
Gene Name
glyA
Organism
Shigella flexneri
Amino acid sequence
>lcl|BSEQ0011317|Serine hydroxymethyltransferase
MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYP
GKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLEPGDTVLGMN
LAHGGHLTHGSPVNFSGKLYNIVPYGIDATGHIDYADLEKQAKEHKPKMIIGGFSAYSGV
VDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLIL
AKGGSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVE
VFLERGYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTS
GIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKGKVLDICARYPVYA
Number of residues
417
Molecular Weight
45316.33
Theoretical pI
6.45
GO Classification
Functions
glycine hydroxymethyltransferase activity / pyridoxal phosphate binding
Processes
glycine biosynthetic process from serine / tetrahydrofolate interconversion
Components
cytoplasm
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011318|Serine hydroxymethyltransferase (glyA)
ATGTTAAAGCGTGAAATGAACATTGCCGATTATGATGCCGAACTGTGGCAGGCTATGGAG
CAGGAAAAAGTACGTCAGGAAGAGCACATCGAACTGATCGCCTCCGAAAACTACACCAGC
CCGCGCGTAATGCAGGCGCAGGGTTCTCAGCTGACCAACAAATATGCTGAAGGTTATCCG
GGCAAACGCTACTACGGCGGTTGCGAGTATGTTGATATCGTTGAACAACTGGCGATCGAT
CGTGCGAAAGAACTGTTCGGCGCTGACTACGCTAACGTCCAGCCGCACTCCGGCTCCCAG
GCTAACTTTGCGGTCTACACCGCGCTGCTGGAACCAGGTGATACCGTTCTGGGTATGAAC
CTGGCGCATGGCGGTCACCTGACTCACGGTTCTCCGGTTAACTTCTCCGGTAAACTGTAC
AACATCGTTCCTTACGGTATCGATGCTACCGGTCATATCGATTACGCCGATCTGGAAAAA
CAAGCCAAAGAACACAAGCCGAAAATGATTATCGGTGGTTTCTCTGCATATTCCGGCGTG
GTTGACTGGGCGAAAATGCGTGAAATCGCTGACAGCATCGGTGCTTATCTGTTCGTTGAT
ATGGCGCACGTTGCGGGCCTGGTTGCTGCTGGCGTCTACCCGAACCCGGTTCCTCATGCT
CACGTTGTTACTACCACCACTCACAAAACCCTGGCGGGTCCGCGCGGCGGCCTGATCTTG
GCGAAAGGTGGTAGCGAAGAGCTGTACAAAAAACTGAACTCTGCCGTTTTCCCTGGTGGT
CAGGGCGGTCCGTTGATGCACGTAATCGCCGGTAAAGCGGTTGCTCTGAAAGAAGCGATG
GAGCCTGAGTTCAAAACTTACCAGCAGCAGGTCGCGAAAAACGCTAAAGCGATGGTAGAA
GTGTTCCTCGAGCGCGGCTACAAAGTGGTTTCCGGCGGCACTGATAACCACCTGTTCCTG
GTTGATCTGGTTGATAAAAACCTGACCGGTAAAGAAGCAGACGCCGCTCTGGGCCGTGCT
AACATCACCGTCAACAAAAACAGCGTACCGAACGATCCGAAGAGCCCGTTTGTGACCTCC
GGTATTCGTGTAGGTACTCCGGCGATTACCCGTCGCGGCTTTAAAGAAGCCGAAGCGAAA
GAACTGGCTGGCTGGATGTGTGACGTGCTGGACAGCATCAATGATGAAGCCGTTATCGAG
CGCATCAAAGGTAAAGTTCTCGACATCTGCGCACGTTACCCGGTTTACGCATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A827
UniProtKB Entry NameGLYA_SHIFL
GenBank Protein ID24052975
GenBank Gene IDAE005674
General References
  1. Jin Q, Yuan Z, Xu J, Wang Y, Shen Y, Lu W, Wang J, Liu H, Yang J, Yang F, Zhang X, Zhang J, Yang G, Wu H, Qu D, Dong J, Sun L, Xue Y, Zhao A, Gao Y, Zhu J, Kan B, Ding K, Chen S, Cheng H, Yao Z, He B, Chen R, Ma D, Qiang B, Wen Y, Hou Y, Yu J: Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157. Nucleic Acids Res. 2002 Oct 15;30(20):4432-41. [Article]
  2. Wei J, Goldberg MB, Burland V, Venkatesan MM, Deng W, Fournier G, Mayhew GF, Plunkett G 3rd, Rose DJ, Darling A, Mau B, Perna NT, Payne SM, Runyen-Janecky LJ, Zhou S, Schwartz DC, Blattner FR: Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T. Infect Immun. 2003 May;71(5):2775-86. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB11596Levoleucovorinapproved, investigationalunknownDetails
DB02824N-Pyridoxyl-Glycine-5-MonophosphateexperimentalunknownDetails