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Q2T437 (GLYA2_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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 2

Short name=SHMT 2
Short name=Serine methylase 2
EC=2.1.2.1
Gene names
Name:glyA2
Ordered Locus Names:BTH_II1868
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length424 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 – 424424Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 2
PRO_0000234961

Regions

Region129 – 1313Substrate binding By similarity

Sites

Binding site391Pyridoxal phosphate By similarity
Binding site591Pyridoxal phosphate By similarity
Binding site611Substrate By similarity
Binding site681Substrate binding By similarity
Binding site691Pyridoxal phosphate By similarity
Binding site1251Substrate By similarity
Binding site1801Pyridoxal phosphate By similarity
Binding site2081Pyridoxal phosphate By similarity
Binding site2331Pyridoxal phosphate By similarity
Binding site2401Pyridoxal phosphate By similarity
Binding site2661Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3661Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2341N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2T437 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 1D83488C8AAE5726

FASTA42445,361
        10         20         30         40         50         60 
MSNANPFFSQ SLAERDASVR GAILKELERQ QSQVELIASE NIVSRAVLDA QGSVLTNKYA 

        70         80         90        100        110        120 
EGYPGKRYYG GCEFADEVEA LAIDRVKQIF NAGHANVQPH SGAQANGAVM LALAKPGDTV 

       130        140        150        160        170        180 
LGMSLDAGGH LTHGAKPALS GKWFNAVQYG VSRDTMLIDY DQVEELAQQH KPSLIIAGFS 

       190        200        210        220        230        240 
AYPRKLDFAR FRAIADSVGA KLMVDMAHIA GVIAAGRHAN PVEHAHVVTS TTHKTLRGPR 

       250        260        270        280        290        300 
GGFVLTNDEE IAKKINSAVF PGLQGGPLMH VIAGKAVAFG EALTDDFKTY IDRVLANAQA 

       310        320        330        340        350        360 
LGDVLKAGGV DLVTGGTDNH LLLVDLRPKG LKGAQVEQAL ERSGITCNKN GIPFDAEKPT 

       370        380        390        400        410        420 
ITSGIRLGTP AGTTRGFGAA EFREVGRLIL EVFDALRTNP AGDHATEQRV RREIFALCER 


FPIY 

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References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000085 Genomic DNA. Translation: ABC35622.1.
RefSeqYP_440062.1. NC_007650.1.

3D structure databases

ProteinModelPortalQ2T437.
SMRQ2T437. Positions 12-410.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2T437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3845012.
GenomeReviewsGene locus BTH_II1868 in contig CP000085_GR.
KEGGbte:BTH_II1868.
PATRIC19301500. VBIBurTha36512_2078.
TIGRBTH_II1868.

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMASHRIDMD.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycBTHA271848:BTH_II1868-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 nameGLYA2_BURTA
AccessionPrimary (citable) accession number: Q2T437
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 44 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