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B3R5S0 (GLYA_CUPTR) 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:RALTA_A2322
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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_1000091535

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
B3R5S0 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 0A5D43F8A4AEDED1

FASTA41545,068
        10         20         30         40         50         60 
MFERSRFTID QIDPEVFAAI QQENQRQEDH IELIASENYT SPAVMAAQGS QLTNKYAEGY 

        70         80         90        100        110        120 
PGKRYYGGCE YVDIVEQLAI DRVKQLFGAE AANVQPNSGS QANQGVYFAV LKPGDTIMGM 

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

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

       250        260        270        280        290        300 
LMKAEHEKAI NSSIFPGIQG GPLMHVIAGK AVAFKEALTP EFKAYQQQVV KNAAVLAETL 

       310        320        330        340        350        360 
IARGLRIVSG RTESHVMLVD LRAKNITGKE AERILGEAHL TVNKNAIPND PEKPFVTSGI 

       370        380        390        400        410 
RVGSPAMTTR GFKEEEARIV GNLIADVLDN PHDAANIAAV REQVSALTKR FPVYG

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633749 Genomic DNA. Translation: CAQ70256.1.
RefSeqYP_002006319.1. NC_010528.1.

3D structure databases

ProteinModelPortalB3R5S0.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3R5S0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6455236.
GenomeReviewsGene locus RALTA_A2322 in contig CU633749_GR.
KEGGcti:RALTA_A2322.
PATRIC21531290. VBICupTai42494_2286.

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_CUPTR
AccessionPrimary (citable) accession number: B3R5S0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 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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