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Q39J72 (GLYA3_BURS3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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 3
Short name=SHMT 3
Short name=Serine methylase 3
EC=2.1.2.1
Gene names
Name:glyA3
Ordered Locus Names:Bcep18194_A3895
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length415 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 – 415415Pyridoxal-phosphate-dependent serine hydroxymethyltransferase 3
PRO_0000234959

Regions

Region126 – 1283Substrate binding By similarity

Sites

Binding site361Pyridoxal phosphate By similarity
Binding site561Pyridoxal phosphate By similarity
Binding site581Substrate By similarity
Binding site651Substrate binding By similarity
Binding site661Pyridoxal phosphate By similarity
Binding site1001Pyridoxal phosphate By similarity
Binding site1221Substrate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2611Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3611Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39J72 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 949B4C6534C0A5B9

FASTA41544,842
        10         20         30         40         50         60 
MFDRAQSTIA NVDPEIFAAI EQENRRQEDH IELIASENYT SPAVMAAQGS QLTNKYAEGY 

        70         80         90        100        110        120 
PGKRYYGGCE YVDVVEQLAI DRVKQLFGAE AANVQPNSGS QANQGVFFAM LKPGDTIMGM 

       130        140        150        160        170        180 
SLAHGGHLTH GSPVNMSGKW FNVVSYGLNE NEDIDYEAAE QLAQEHKPKL IVAGASAFSL 

       190        200        210        220        230        240 
KIDFERLAKI AKSVGAYLMV DMAHYAGLIA AGVYPNPVPH ADFVTTTTHK SLRGPRGGVI 

       250        260        270        280        290        300 
LMKAEYEKPI NSAIFPGIQG GPLMHVIAGK AVAFKEALSP EFKAYQEKVV ENARVLAETL 

       310        320        330        340        350        360 
VKRGLRIVSG RTESHVMLVD LRAKHITGKA AEAALGAAHI TVNKNAIPND PEKPFVTSGV 

       370        380        390        400        410 
RLGSPAMTTR GFGPAEAEQV GNLIADVLDN PEDAATIERV RAQVAELTKR FPVYR

« Hide

References

[1]"Complete sequence of chromosome 1 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		CP000151 Genomic DNA. Translation: ABB07494.1.
RefSeqYP_368138.1. NC_007510.1.

3D structure databases

ProteinModelPortalQ39J72.
SMRQ39J72. Positions 4-414.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39J72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3749080.
GenomeReviewsGene locus Bcep18194_A3895 in contig CP000151_GR.
KEGGbur:Bcep18194_A3895.
NMPDRfig|269483.3.peg.4639.
PATRIC19285116. VBIBurSp120713_1989.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHBG301263.
OMARIDFERI.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_A3895-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 nameGLYA3_BURS3
AccessionPrimary (citable) accession number: Q39J72
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 47 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

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