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Q8K9P2 (GLYA_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_278
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

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 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 – 417417Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_0000113548

Regions

Region125 – 1273Substrate binding By similarity

Sites

Binding site351Pyridoxal phosphate By similarity
Binding site551Pyridoxal phosphate By similarity
Binding site571Substrate By similarity
Binding site641Substrate binding By similarity
Binding site651Pyridoxal phosphate By similarity
Binding site991Pyridoxal phosphate By similarity
Binding site1211Substrate By similarity
Binding site1751Pyridoxal phosphate By similarity
Binding site2031Pyridoxal phosphate By similarity
Binding site2281Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3631Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2291N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9P2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 78EA4A422A7FF375

FASTA41746,432
        10         20         30         40         50         60 
MFNTKIEFSK YDPELWKAID QEKNRQENHI ELIASENYTS NYVMHVQGSQ LTNKYAEGYP 

        70         80         90        100        110        120 
EKRYYGGCKY VDIIEKLAIN RAKKLFNADY ANVQPHSGSQ ANFAVYTALL NPGDTILGMK 

       130        140        150        160        170        180 
LSHGGHLTHG SSVNFSGKTY NVIGYGVDKK GNIDYQEILT LAKKYKPKMI IGGFSAYSGI 

       190        200        210        220        230        240 
CNWSKMRDIA DEINAYFVVD IAHVAGLIAA NLYPNPIDYA HVVTSTTHKT LAGPRGGLIL 

       250        260        270        280        290        300 
AKNGTNTFYK KINLSVFPGA QGGPLMHVIA AKAIAFKEAL EPAFKIYQKQ VIKNAQVMVQ 

       310        320        330        340        350        360 
SFLKKDYQIV SGNTFNHLFL LDLTSKNITG QEADIALGKC NITVNKNTIP NDLRSPFITS 

       370        380        390        400        410 
GIRIGTPAVT KRGFKENEML QISDWIVHIL NNIKDKNSLL GIKNEVLKLC SKYPVYI

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013218 Genomic DNA. Translation: AAM67836.1.
RefSeqNP_660625.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9P2.
SMRQ8K9P2. Positions 1-416.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000000145; EBBUCP00000000145; EBBUCG00000000145.
GeneID1005482.
GenomeReviewsGene locus BUsg_278 in contig AE013218_GR.
KEGGbas:BUsg278.
PATRIC21247361. VBIBucAph100086_0290.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000008150.
HOGENOMHBG301263.
OMAKAICAKF.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycBAPH198804:BUSG278-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 nameGLYA_BUCAP
AccessionPrimary (citable) accession number: Q8K9P2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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