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Q0TET8 (GLYA_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Serine hydroxymethyltransferase

Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:ECP_2552
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_00051

Catalytic activity

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine. HAMAP-Rule MF_00051

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00051

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_00051

Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. HAMAP-Rule MF_00051

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00051

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00051.

Sequence similarities

Belongs to the SHMT family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
One-carbon metabolism
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionTransferase
   PTMAcetylation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycine biosynthetic process from serine

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglycine hydroxymethyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_1000006246

Regions

Region125 – 1273Substrate binding By similarity
Region355 – 3573Substrate binding By similarity

Sites

Binding site351Pyridoxal phosphate By similarity
Binding site551Pyridoxal phosphate By similarity
Binding site571Substrate By similarity
Binding site641Substrate By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site991Pyridoxal phosphate By similarity
Binding site1211Substrate; via carbonyl oxygen By similarity
Binding site1751Pyridoxal phosphate By similarity
Binding site2031Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3631Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue541N6-acetyllysine By similarity
Modified residue2291N6-(pyridoxal phosphate)lysine By similarity
Modified residue2501N6-acetyllysine By similarity
Modified residue2851N6-acetyllysine By similarity
Modified residue3541N6-acetyllysine By similarity
Modified residue3751N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0TET8 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 13E5558E99938539

FASTA41745,317
        10         20         30         40         50         60 
MLKREMNIAD YDAELWQAME QEKVRQEEHI ELIASENYTS PRVMQAQGSQ LTNKYAEGYP 

        70         80         90        100        110        120 
GKRYYGGCEY VDIVEQLAID RAKELFGADY ANVQPHSGSQ ANFAVYTALL EPGDTVLGMN 

       130        140        150        160        170        180 
LAHGGHLTHG SPVNFSGKLY NIVPYGIDAT GHIDYADLEK QAKEHKPKMI IGGFSAYSGV 

       190        200        210        220        230        240 
VDWAKMREIA DSIGAYLFVD MAHVAGLVAA GVYPNPVPHA HVVTTTTHKT LAGPRGGLIL 

       250        260        270        280        290        300 
AKGGSEELYK KLNSAVFPGG QGGPLMHVIA GKAVALKEAM EPEFKTYQQQ VAKNAKAMVE 

       310        320        330        340        350        360 
VFLERGYKVV SGGTDNHLFL VDLVDKNLTG KEADAALGRA NITVNKNSVP NDPKSPFVTS 

       370        380        390        400        410 
GIRVGTPAIT RRGFKEAEAK ELAGWMCDVL DSINDEAVIE RIKGKVLDIC ARYPVYA 

« Hide

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000247 Genomic DNA. Translation: ABG70541.1.
RefSeqYP_670442.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0TET8.
SMRQ0TET8. Positions 1-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362663.ECP_2552.

Proteomic databases

PRIDEQ0TET8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG70541; ABG70541; ECP_2552.
GeneID4190758.
KEGGecp:ECP_2552.
PATRIC18195907. VBIEscCol77757_2590.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239404.
KOK00600.
OMAKEMYDLE.
OrthoDBEOG6Z0QB2.
PhylomeDBQ0TET8.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycECOL362663:GIY5-2565-MONOMER.
UniPathwayUPA00193.
UPA00288; UER01023.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00051. SHMT.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERPTHR11680. PTHR11680. 1 hit.
PfamPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFPIRSF000412. SHMT. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA_ECOL5
AccessionPrimary (citable) accession number: Q0TET8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: February 19, 2014
This is version 58 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

PATHWAY comments

Index of metabolic and biosynthesis pathways