Skip Header

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

A2REH5 (GLYA_STRPG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. 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:
Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:SpyM50923
OrganismStreptococcus pyogenes serotype M5 (strain Manfredo) [Complete proteome] [HAMAP]
Taxonomic identifier160491 [NCBI]
Taxonomic lineageBacteria › Firmicutes › 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 serving as the one-carbon carrier By similarity.

Catalytic activity

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

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_00051

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP MF_00051

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_00051.

Sequence similarities

Belongs to the SHMT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000006331

Regions

Region125 – 1273Substrate binding By similarity

Sites

Binding site351Pyridoxal phosphate By similarity
Binding site551Pyridoxal phosphate By similarity
Binding site571Substrate By similarity
Binding site641Substrate binding By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site991Pyridoxal phosphate By similarity
Binding site1211Substrate 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
A2REH5 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 6C512624D7937161

FASTA41845,080
        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 
SIDFEKFRAI ADHVGAYLMV DMAHIAGLVA AGVHPSPVPY AHIVTSTTHK TLRGPRGGLI 

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

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

       370        380        390        400        410 
GIRIGCAAIT SRGMGVKESQ TIARLIIKAL VNHDQETILE EVRQEVRQLT DAFPLYKK

« Hide

References

[1]"Complete genome of acute rheumatic fever-associated serotype M5 Streptococcus pyogenes strain Manfredo."
Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S., Skelton J. expand/collapse author list , Whitehead S., Barrell B.G., Kehoe M., Parkhill J.
J. Bacteriol. 189:1473-1477(2007) [PubMed: 17012393] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Manfredo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM295007 Genomic DNA. Translation: CAM30250.1.
RefSeqYP_001128480.1. NC_009332.1.

3D structure databases

ProteinModelPortalA2REH5.
SMRA2REH5. Positions 12-411.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2REH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000048177; EBSTRP00000046305; EBSTRG00000048169.
GeneID4963362.
GenomeReviewsGene locus SpyM50923 in contig AM295007_GR.
KEGGspf:SpyM50923.
PATRIC19765014. VBIStrPyo41547_0962.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
GeneTreeEBGT00050000027108.
HOGENOMHBG301263.
OMAFSASYEM.
ProtClustDBPRK00011.

Family and domain databases

HAMAPMF_00051. SHMT.
[Tree]
InterProIPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KOK00600.
PANTHERPTHR11680. Gly_HO-Metrfase. 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_STRPG
AccessionPrimary (citable) accession number: A2REH5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: January 25, 2012
This is version 38 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