Skip Header

Contribute Send feedback
Read comments (?) or add your own

P0DF70 (GLYA_STRP3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 18. 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
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:SpyM3_0803
OrganismStreptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315) [Complete proteome] [HAMAP]
Taxonomic identifier198466 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length418 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
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycine biosynthetic process from serine

Inferred from electronic annotation. Source: 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: HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_0000113677

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 site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2621Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3631Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0DF70 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: 1CA3D5E167C13650

FASTA41845,079
        10         20         30         40         50         60 
MIFDKGNVED FDKELWDAIH AEEERQEHHI ELIASENMVS KAVMAAQGSV LTNKYAEGYP 

        70         80         90        100        110        120 
GNRYYGGTEC VDIVETLAIE RAKKLFGAAF ANVQAHSGSQ ANAAAYMALI EAGDTVLGMD 

       130        140        150        160        170        180 
LAAGGHLTHG SPVNFSGKTY HFVGYSVDAD TEMLNYEAIL EQAKAVQPKL IVAGASAYSR 

       190        200        210        220        230        240 
NIDFEKFRAI ADHVGAYLMV DMAHIAGLVA AGVHPSPVPY AHIVTSTTHK TLRGPRGGLI 

       250        260        270        280        290        300 
LTNDEALAKK INSAVFPGLQ GGPLEHVIAA KAVAFKEALD PAFKDYAQAI IDNTAAMAAV 

       310        320        330        340        350        360 
FAQDDRFRLI SGGTDNHVFL VDVTKVIANG KLAQNLLDEV NITLNKNAIP FETLSPFNTS 

       370        380        390        400        410 
GIRIGCAAIT SRGMGVKESQ TIARLIIKAL VNHDQETILE EVRQEVRQLT DAFPLYKK

« Hide

References

[1]"Genome sequence of a serotype M3 strain of group A Streptococcus: phage-encoded toxins, the high-virulence phenotype, and clone emergence."
Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D., Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S., Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-595 / MGAS315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014074 Genomic DNA. Translation: AAM79410.1.
RefSeqNP_664607.1. NC_004070.1.

3D structure databases

ProteinModelPortalP0DF70.
SMRP0DF70. Positions 12-411.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM79410; AAM79410; SpyM3_0803.
GeneID1009117.
KEGGspg:SpyM3_0803.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000239404.
KOK00600.
OMAERFRAIC.

Enzyme and pathway databases

BioCycSPYO198466:GJDL-864-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. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA_STRP3
AccessionPrimary (citable) accession number: P0DF70
Secondary accession number(s): Q8K7H8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 27, 2011
Last modified: May 29, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents