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A8AXC8 (GLYA_STRGC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:SGO_1151
OrganismStreptococcus gordonii (strain Challis / ATCC 35105 / CH1 / DL1 / V288) [Complete proteome] [HAMAP]
Taxonomic identifier29390 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length420 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 – 420420Pyridoxal-phosphate-dependent serine hydroxymethyltransferase
PRO_1000074915

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 site1761Pyridoxal phosphate By similarity
Binding site2041Pyridoxal phosphate By similarity
Binding site2291Pyridoxal phosphate By similarity
Binding site2361Pyridoxal phosphate By similarity
Binding site2621Pyridoxal 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
A8AXC8 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: CBE56555C05ACF93

FASTA42045,538
        10         20         30         40         50         60 
MIFDQEDYKA FDPEIWEAVA KEEERQQHNI ELIASENVVS KAVMAAQGSI LTNKYAEGYP 

        70         80         90        100        110        120 
GRRYYGGTDV VDVIESLAIE RAKEIFGAKF ANVQPHSGSQ ANCAAYMALI EPGDTVMGMD 

       130        140        150        160        170        180 
LSAGGHLTHG ASVSFSGQTY NFVSYSVDPE TELLDFDAIL KQAKEVQPKL IVAGASAYSH 

       190        200        210        220        230        240 
IIDFSKFREI ADAVGAKLMV DMAHIAGLVA AGLHPSPVPY ADITTTTTHK TLRGPRGGLI 

       250        260        270        280        290        300 
LTNDEDLAKK INSAIFPGIQ GGPLEHVIAA KAVAFKEVLD PAFKVYAQQI LDNAQAMAQV 

       310        320        330        340        350        360 
FRQHDKFRVI SDGTENHLFL VDVTKVVENG KVAQNLLDEV NITLNKNSIP YETLSPFKTS 

       370        380        390        400        410        420 
GIRIGTAAIA ARGFGVTESI KVAELIIKAL ENAENEAVLN QVRAEVRELT DAFPLYEGLN

« Hide

References

[1]"Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide."
Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.
J. Bacteriol. 189:7799-7807(2007) [PubMed: 17720781] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Challis / ATCC 35105 / CH1 / DL1 / V288.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000725 Genomic DNA. Translation: ABV09592.1.
RefSeqYP_001450438.1. NC_009785.1.

3D structure databases

ProteinModelPortalA8AXC8.
SMRA8AXC8. Positions 12-411.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000011679; EBSTRP00000011236; EBSTRG00000011679.
GeneID5598919.
GenomeReviewsGene locus SGO_1151 in contig CP000725_GR.
KEGGsgo:SGO_1151.
PATRIC19660261. VBIStrGor124371_1137.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000027108.
HOGENOMHBG301263.
OMARGMGAKE.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycSGOR29390:SGO_1151-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_STRGC
AccessionPrimary (citable) accession number: A8AXC8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 35 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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