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Q39A26 (GLYA1_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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 1

Short name=SHMT 1
Short name=Serine methylase 1
EC=2.1.2.1
Gene names
Name:glyA1
Ordered Locus Names:Bcep18194_B0571
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

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 1
PRO_0000234957

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
Q39A26 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 7F1451934ECC5E51

FASTA42445,454
        10         20         30         40         50         60 
MSNTQPFFSQ PLAERDAPVR SAILKELERQ QSQVELIASE NIVSRAVLEA QGSVLTNKYA 

        70         80         90        100        110        120 
EGYPGKRYYG GCEFADEVEA LAIDRVKQIF NAGYANVQPH SGAQANGSVM LALAKPGDTV 

       130        140        150        160        170        180 
LGMSLDAGGH LTHGAKPALS GKWFNAVQYG VNRDTMLIDY DQVEALAHEH KPNLIIAGFS 

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

       250        260        270        280        290        300 
GGFVLTNDED IAKKINSAVF PGLQGGPLMH VIAGKAVAFG EVLQADFKTY IDNVLANAQA 

       310        320        330        340        350        360 
LGEVLKAGGV DLVTGGTDNH LLLVDLRPKG LKGAPVEQAL ERAGITCNKN GIPFDTEKPT 

       370        380        390        400        410        420 
VTSGIRLGTP AGTTRGFGVA EFREVGRLIL EVFDALRANP EGDHATEQRV RREIFALCER 


FPIY 

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References

[1]"Complete sequence of chromosome 2 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000152 Genomic DNA. Translation: ABB10685.1.
RefSeqYP_371329.1. NC_007511.1.

3D structure databases

ProteinModelPortalQ39A26.
SMRQ39A26. Positions 12-389.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39A26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3752335.
GenomeReviewsGene locus Bcep18194_B0571 in contig CP000152_GR.
KEGGbur:Bcep18194_B0571.
NMPDRfig|269483.3.peg.805.
PATRIC19291854. VBIBurSp120713_5292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMAIFNAGYA.
ProtClustDBPRK13034.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_B0571-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 nameGLYA1_BURS3
AccessionPrimary (citable) accession number: Q39A26
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 46 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