Skip Header

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

B1IBI3 (GLYA_STRPI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:SPH_1127
OrganismStreptococcus pneumoniae (strain Hungary19A-6) [Complete proteome] [HAMAP]
Taxonomic identifier487214 [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_1000091586

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
B1IBI3 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: CD5EF4416AEF057E

FASTA41845,254
        10         20         30         40         50         60 
MIFDKDDFKA YDADLWNAIA KEEERQQNNI ELIASENVVS KAVMAAQGSI LTNKYAEGYP 

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

       130        140        150        160        170        180 
LASGGHLTHG APVSFSGQTY NFVSYSVDPE 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 DAFPLYEE

« Hide

References

[1]"Complete sequence of Streptococcus pneumoniae strain Hungary 19A-6."
Hotopp J.D., Censini S., Masignani V., Covacci A., Tettelin H.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hungary19A-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000936 Genomic DNA. Translation: ACA37237.1.
RefSeqYP_001694468.1. NC_010380.1.

3D structure databases

ProteinModelPortalB1IBI3.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1IBI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000024690; EBSTRP00000023856; EBSTRG00000024690.
GeneID6029577.
GenomeReviewsGene locus SPH_1127 in contig CP000936_GR.
KEGGspv:SPH_1127.
PATRIC19692372. VBIStrPne34925_1138.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000027108.
HOGENOMHBG301263.
OMARGMGAKE.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycSPNE487214:SPH_1127-MONOMER.

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_STRPI
AccessionPrimary (citable) accession number: B1IBI3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 31 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