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B2U7G7 (GLYA_RALPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:Rpic_0678
OrganismRalstonia pickettii (strain 12J) [Complete proteome] [HAMAP]
Taxonomic identifier402626 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia

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
PRO_1000091571

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
B2U7G7 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 584661FB2328D224

FASTA41544,913
        10         20         30         40         50         60 
MFERSRYTID QIDPEIFAAI QKENQRQEDH IELIASENYT SPAVMAAQGS QLTNKYAEGY 

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

       130        140        150        160        170        180 
SLAEGGHLTH GMALNMSGKW FNVVSYGLNA QEDIDYDALE ALAQEKKPKL IIAGASAFAL 

       190        200        210        220        230        240 
RIDFERIGKI AKSIGAYFMV DMAHYAGLIA AGVYPNPVPH ADFVTTTTHK SLRGPRGGVI 

       250        260        270        280        290        300 
LMKAEHEKAI NSAIFPGIQG GPLMHVIAGK AVAFKEALSP EFKAYQEQVV KNAAAMAETL 

       310        320        330        340        350        360 
MARGLRIVSG RTESHVMLVD LRAKKITGKE AEKVLGDAHI TVNKNAIPND PEKPFVTSGV 

       370        380        390        400        410 
RLGSPAMTTR GFKEAEAVKV AHLIADVLDN PHDEANIAAV RAKVAELTKQ FPVYG

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia pickettii 12J."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marsh T., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12J.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001068 Genomic DNA. Translation: ACD25829.1.
RefSeqYP_001898261.1. NC_010682.1.

3D structure databases

ProteinModelPortalB2U7G7.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2U7G7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6288856.
GenomeReviewsGene locus Rpic_0678 in contig CP001068_GR.
KEGGrpi:Rpic_0678.
PATRIC20252216. VBIRalPic63053_1875.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG301263.
OMARIDFERI.
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_RALPJ
AccessionPrimary (citable) accession number: B2U7G7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 28 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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