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Q14GZ5 (GLYA_FRAT1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine hydroxymethyltransferase

Short name=SHMT
Short name=Serine methylase
EC=2.1.2.1
Gene names
Name:glyA
Ordered Locus Names:FTF1241
OrganismFrancisella tularensis subsp. tularensis (strain FSC 198) [Complete proteome] [HAMAP]
Taxonomic identifier393115 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism By similarity. HAMAP-Rule MF_00051

Catalytic activity

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine. HAMAP-Rule MF_00051

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00051

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_00051

Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. HAMAP-Rule MF_00051

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00051

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00051.

Sequence similarities

Belongs to the SHMT family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
One-carbon metabolism
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycine biosynthetic process from serine

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglycine hydroxymethyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Serine hydroxymethyltransferase HAMAP-Rule MF_00051
PRO_1000006250

Regions

Region126 – 1283Substrate binding By similarity
Region355 – 3573Substrate binding By similarity

Sites

Binding site361Pyridoxal phosphate By similarity
Binding site561Pyridoxal phosphate By similarity
Binding site581Substrate By similarity
Binding site651Substrate By similarity
Binding site661Pyridoxal phosphate By similarity
Binding site1001Pyridoxal phosphate By similarity
Binding site1221Substrate; via carbonyl oxygen By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3631Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q14GZ5 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 419A2B83E0C8DB03

FASTA41745,316
        10         20         30         40         50         60 
MFSFEKNSLK NTDKEIFDAI ELEVKRQHEH VELIASENYA SPAVMEAQGS QLTNKYAEGY 

        70         80         90        100        110        120 
HGKRYYGGCE FVDIAEKLAI ERAQQLFGVD YANVQPHSGS QANAAVYNAV LKPGDTVLGM 

       130        140        150        160        170        180 
DLGAGGHLTH GSKVNFSGKI YNSIQYGLDE NGDIDYKQVA QLAKEHKPKM IIAGFSAFSG 

       190        200        210        220        230        240 
IINWQKFREI ADSVDAVLMA DIAHVAGLVA AGVYPNPFPY VYVATTTTHK TLRGPRGGLI 

       250        260        270        280        290        300 
LCNNNPELAK KFQSAIFPGI QGGPLMHVIA AKAVAFKEAL EPSFVDYQKQ VLKNAKAMEK 

       310        320        330        340        350        360 
VLKQRGINII SGGTSNHLLL LDITNTGFSG KEAEAALGRA NITVNKNSIP NDPRSPFVTS 

       370        380        390        400        410 
GLRIGSPAIT TRGFKEKECE LVANLLADVV FNCGDEKVEN ETAAKVLDLC DKFPVYK 

« Hide

References

[1]"Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FSC 198.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286280 Genomic DNA. Translation: CAL09257.1.
RefSeqYP_667331.1. NC_008245.1.

3D structure databases

ProteinModelPortalQ14GZ5.
SMRQ14GZ5. Positions 8-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393115.FTF1241.

Proteomic databases

PRIDEQ14GZ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL09257; CAL09257; FTF1241.
GeneID4200288.
KEGGftf:FTF1241.
PATRIC17961544. VBIFraTul133500_1434.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239404.
KOK00600.
OMAMLIDLRN.
OrthoDBEOG6Z0QB2.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycFTUL393115:GJUT-1259-MONOMER.
UniPathwayUPA00193.
UPA00288; UER01023.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00051. SHMT.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERPTHR11680. PTHR11680. 1 hit.
PfamPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFPIRSF000412. SHMT. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLYA_FRAT1
AccessionPrimary (citable) accession number: Q14GZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways