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Q04KR0 (GLYA_STRP2) 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
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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:SPD_0910
OrganismStreptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) [Complete proteome] [HAMAP]
Taxonomic identifier373153 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

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_1000006327

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
Q04KR0 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 97D07D488FDF8250

FASTA41845,256
        10         20         30         40         50         60 
MIFDKDDFKA YDADLWNAIA KEEERQQNNI ELIASENVVS KAVMAAQGSI LTNKYAEGYP 

        70         80         90        100        110        120 
GRRYYGGTDV VDVVETLAIE RAKEIFGAKF ANVQPHSGSQ ANCAAYMSLI EPGDTVMGMD 

       130        140        150        160        170        180 
LAAGGHLTHG APVSFSGQTY NFLSYSVDPE TELLDFDAIL KQAQEVKPKL IVAGASAYSQ 

       190        200        210        220        230        240 
IIDFSKFREI ADAVGAKLMV DMAHIAGLVA AGLHPSPVPY AHITTTTTHK TLRGPRGGLI 

       250        260        270        280        290        300 
LTNDEELAKK INSAIFPGIQ GGPLEHVVAA KAVSFKEVLD PAFKEYAANV IKNSKAMADV 

       310        320        330        340        350        360 
FLQDPDFRII SGGTENHLFL VDVTKVVENG KVAQNLLDEV NITLNKNSIP YETLSPFKTS 

       370        380        390        400        410 
GIRIGAAAIT ARGFGEEESR KVAELIIKTL KNSENEAVLE EVRSAVKELT DAFPLYED 

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References

[1]"Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6."
Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.
J. Bacteriol. 189:38-51(2007) [PubMed: 17041037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D39 / NCTC 7466.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000410 Genomic DNA. Translation: ABJ55301.1.
RefSeqYP_816388.1. NC_008533.1.

3D structure databases

ProteinModelPortalQ04KR0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ04KR0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000019709; EBSTRP00000018949; EBSTRG00000019709.
GeneID4441989.
GenomeReviewsGene locus SPD_0910 in contig CP000410_GR.
KEGGspd:SPD_0910.
PATRIC19682971. VBIStrPne27904_1021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
GeneTreeEBGT00050000027108.
HOGENOMHBG301263.
OMARGMGAKE.
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_STRP2
AccessionPrimary (citable) accession number: Q04KR0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
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