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Q1JGU8 (GLYA_STRPD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

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

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:MGAS10270_Spy0981
OrganismStreptococcus pyogenes serotype M2 (strain MGAS10270) [Complete proteome] [HAMAP]
Taxonomic identifier370552 [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_1000006330

Regions

Region127 – 1293Substrate binding By similarity

Sites

Binding site371Pyridoxal phosphate By similarity
Binding site571Pyridoxal phosphate By similarity
Binding site591Substrate By similarity
Binding site661Substrate binding By similarity
Binding site671Pyridoxal phosphate By similarity
Binding site1011Pyridoxal phosphate By similarity
Binding site1231Substrate By similarity
Binding site1781Pyridoxal phosphate By similarity
Binding site2061Pyridoxal phosphate By similarity
Binding site2311Pyridoxal phosphate By similarity
Binding site2381Pyridoxal phosphate By similarity
Binding site2641Pyridoxal phosphate; via amide nitrogen and carbonyl oxygen By similarity
Binding site3651Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2321N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1JGU8 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 8BD77B75D17E0DB8

FASTA42045,338
        10         20         30         40         50         60 
MTMIFDKGNV EDFDKELWDA IHAEEERQEH HIELIASENM VSKAVMAAQG SVLTNKYAEG 

        70         80         90        100        110        120 
YPGNRYYGGT ECVDIVETLA IERAKKLFGA AFANVQAHSG SQANAAAYMA LIEAGDTVLG 

       130        140        150        160        170        180 
MDLAAGGHLT HGSPVNFSGK TYHFVGYSVD ADTEMLNYEA ILEQAKAVQP KLIVAGASAY 

       190        200        210        220        230        240 
SRSIDFEKFR AIADHVDAYL MVDMAHIAGL VAAGVHPSPV PYAHIVTSTT HKTLRGPRGG 

       250        260        270        280        290        300 
LILTNDEALA KKINSAVFPG LQGGPLEHVI AAKAVAFKEA LDPAFKDYAQ AIIDNTAAMA 

       310        320        330        340        350        360 
AVFAQDDRFR LISGGTDNHV FLVDVTKVIA NGKLAQNLLD EVNITLNKNA IPFETLSPFK 

       370        380        390        400        410        420 
TSGIRIGCAA ITSRGMGVKE SQTIAHLIIK ALVNHDQETI LEEVRQEVRQ LTDAFPLYKK

« Hide

References

[1]"Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus."
Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed: 16636287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS10270.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000260 Genomic DNA. Translation: ABF34046.1.
RefSeqYP_598590.1. NC_008022.1.

3D structure databases

ProteinModelPortalQ1JGU8.
SMRQ1JGU8. Positions 14-413.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1JGU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000040969; EBSTRP00000039453; EBSTRG00000040966.
GeneID4064441.
GenomeReviewsGene locus glyA in contig CP000260_GR.
KEGGsph:MGAS10270_Spy0981.
PATRIC19719884. VBIStrPyo120482_0999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0112.
GeneTreeEBGT00050000027108.
HOGENOMHBG301263.
OMAFSASYEM.
ProtClustDBPRK00011.

Enzyme and pathway databases

BioCycSPYO370552:MGAS10270_SPY0981-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_STRPD
AccessionPrimary (citable) accession number: Q1JGU8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 13, 2006
Last modified: January 25, 2012
This is version 44 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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